Nucleic acids of aspergillus fumigatus encoding industrial enzymes and methods of use

ABSTRACT

The present invention provides nucleotide sequences of  Aspegillus fumigatus  that encode proteins which exhibit enzyme activities. Vectors, expression constructs, and host cells comprising the nucleotide sequences of the enzyme genes are also provided. The invention further provides methods for producing the enzymes, and methods for modifying the enzymes in order to improve their desirable characteristics. The activities displayed by the enzymes of the invention include those of a tannase, cellulase, glucose oxidase, glucoamylase, phytase, β-galactosidases, invertase, lipase, α-amylase, laccase, polygalacturonase or xylanase. The enzymes of the invention can be used in a variety of industrial processes. Enzymatically active compositions in various forms as well as antibodies to the enzymes and fragments thereof, are also provided.

1. INTRODUCTION

[0001] The present invention is directed toward isolated nucleic acids of Aspergillus fumigatus that encode enzymes with industrial applications, and methods of uses.

2. BACKGROUND OF THE INVENTION

[0002] Enzymatic processes enable natural raw materials to be refined and/or converted into useful intermediates or finished products. Historically, enzymatic processes had been used for the production of foodstuffs and flavorings. During traditional koji fermentation in China and Japan, various filamentous fungi such as Aspergillus oryzae and Aspergillus sojae have been used to make soy sauce, miso (soyabean paste) and sake wine. Jokichi Takamine was awarded U.S. Pat. No. 525,823 in 1894 for the first microbial enzyme, an α-amylase from A. oryzae, to be manufactured for commerce.

[0003] In 1960's and 1970's, several different enzymes, such as amyloglucosidases (AMG by Novo Nordisk, DIAZYME by Solvay) and glucose isomerases (SPEZYME by Genencor, SWEETZYME by Novo Nordisk) became widely used for converting starch from various natural sources into a range of syrups. Many other types of enzymes are now being used in the wine and juice industries, bakeries, and in the cheese industry. See Bigelis, R. “Food enzymes” in “Biotechnology of filamentous fungi”, ed. by Finkelstein and Ball, 1992, Butterworth-Heinemann.

[0004] Enzymes are also extensively used in the textile and leather industries which uses various enzymes to desize textile fibers and to make soft and supple leather from rawhides. In the detergent industry, several generations of proteases with desirable properties such as a high pH optimum and stability have been developed in the last 30 years, e.g., ESPERASE in 1974 by Novo Nordisk, and OPTICLEAN in 1982 by Solvay. Lipase and cellulase type detergent enzymes have also been developed, e.g., CELLUZYME and LIPOLASE both by Novo Nordisk. In recent years, enzymes for use in detergents based on genetic engineering techniques were introduced, e.g., SUBTILISIN NOVO (Genencor), and bleach-stable high pH proteases MAXAPEM by IBIS.

[0005] Worldwide consumption of industrial enzymes amounted to approximately $720 million in 1990. The growth in volume of the enzyme business from 1980 to 1990 was estimated to be 5-10% per year. Overall, the starch conversion and detergent industries are by far the most important consumers. The other major uses are in the dairy, textile, and alcohol-making industries.

[0006] The synthesis of polymers, pharmaceuticals, natural products and agrochemicals is often hampered by expensive processes which produce harmful byproducts and which suffer from low selectivity with respect to optical isomers. Enzymes have a number of remarkable advantages which can overcome many of the current problems in catalysis: they act on single functional groups, they distinguish between similar functional groups on a single molecule, they distinguish between enantiomers, and they function at very low mole fractions in reaction mixtures. Because of the specificity of their actions, enzymes present a unique solution to achieve selective transformations which are often extremely difficult to duplicate chemically. The elimination of the need for protection groups, selectivity, the ability to carry out multi-step transformations in a single reaction vessel, has led to an increased demand for enzymes in chemical and pharmaceutical industries. A current limitation to more widespread industrial use is primarily due to the relatively small number of commercially available enzymes.

[0007] The industrial use of enzymes is also an important contribution to the development of environment-friendly technology. They replace conventional chemical-based technologies and energy-intensive manufacturing processes. They originate from natural biological systems and are therefore totally biodegradable. Generally, enzymatic processes require less energy, less equipment or fewer chemicals.

[0008] As the need for better catalysts and the interest in using environment-friendly processes grow, there is an emerging need for more effective and robust enzymes for a variety of industries. So far, enzymes of commercial interest have been obtained from several Aspergillus species, such as, A. niger, A. oryzae, A. awamori, A. alliaceus, A. usamii, A. ficum, A. saitoi, and A. melleus.

[0009]Aspergillus fumigatus is a saprophytic fungus that plays an essential role in recycling environmental carbon and nitrogen. Its natural ecological niche is the soil, wherein it survives and grows on organic debris. Although this species is not the most prevalent fungus in the world, it is one of the most ubiquitous of those with airborne conidia. Inhalation of the conidia by an immunosuppressed individual often leads to an opportunistic infection with A. fumigatus which is severe and can be fatal. It is the most common etiological agent of Aspergillus infections in humans. However, unlike the other Aspergillus species, very little is known about the enzymes of A. fumigatus. U.S. Pat. No. 4,593,005 discloses amylolytic enzymes from an Aspergillus strain that share some morphological characteristics with A. fumigatus.

[0010] The present invention takes a genomics approach to identify enzymes in Aspergillus fumigatus that can be used in industrial processes. Citation or discussion of a reference herein shall not be construed as an admission that such is prior art to the present invention.

3. SUMMARY OF THE INVENTION

[0011] The present invention provides the nucleotide sequences of twenty four enzyme genes of Aspergillus fumigatus. The enzyme genes encode a protein with an enzyme activity that is either in use in an industry or of interest to an industry. The genomic sequences of the invention that encode the enzymes are identified primarily by comparison of nucleotide sequences of A. fumigatus genomic DNA and the nucleotide sequences of known enzyme genes of other microorganisms. Prior to this invention, the nucleotide sequences of these A. fumigatus genes, the reading frames, the positions of exons and introns, the structure of the enzymes, and their potential usefulness in various industries, such as those involved in the making of food and feed, beverages, textiles and detergents, were not known. Without limitation, the polynucleotides of the enzyme genes can be used to express recombinant enzymes for characterization, modifications or industrial uses; to compare with the nucleic acid sequence of Aspergillus fumigatus to identify duplicated genes or paralogs having the same or similar biochemical activity and/or function; to compare with nucleic acid sequences of other related or distant fungal organisms to identify potential orthologous enzyme genes; for selecting and making oligomers for attachment to a nucleic acid array for examination of expression patterns; and to raise anti-protein antibodies using nucleic acid immunization techniques. The sequence information provided herein can also form a basis for the design and testing of genetically modified enzymes which possess desirable chemical and physical characteristics.

[0012] In one embodiment, the invention provides isolated nucleic acids that encode tannases (SEQ ID NO: 1, 2, 4, and 5), a cellulase (SEQ ID NO: 7 and 8), glucose oxidases (SEQ ID NO: 10, 11, 13, 14, 16, and 17), glucoamylases (SEQ ID NO: 19, 20, 31, 32, 52 and 53), a phytase (SEQ ID NO: 22 and 23), β-galactosidases (SEQ ID NO: 25, 26, 28, and 29), a sucrase or invertase (SEQ ID NO: 34 and 35), a lipase (SEQ ID NO: 37 and 38), α-amylases (SEQ ID NO: 40, 41, 43, 44, 46, and 47), a laccase (SEQ ID NO: 49, and 50), polygalacturonases (SEQ ID NO: 55, 56, 58, 59, 61 and 62), and xylanases (SEQ ID NO: 64, 65, 67, 68, 70 and 71). For each gene of the invention, an open reading frame (ORF) sequence was derived manually from the respective genomic sequence by deleting predicted intron sequences and splicing together exon sequences. Vectors, expression vectors, and host cells comprising the enzyme genes are also encompassed.

[0013] In another embodiment, the invention provides deduced amino acid sequences of enzymes that are predicted from the ORF sequences of the enzyme genes. Based on the sequence conservation displayed between the Aspergillus fumigatus genes of the invention and their homologs in other fungi, it is predicted that the polypeptides encoded by these A. fumigatus genes exhibit enzymatic activities similar to their homologs. The amino acid sequences of the invention correspond to those of tannases (SEQ ID NO: 3 and 6), cellulase (SEQ ID NO: 9), glucose oxidases (SEQ ID NO: 12, 15, and 18), glucoamylases (SEQ ID NO: 21, 33 and 57), phytase (SEQ ID NO: 24), β-galactosidases (SEQ ID NO: 27 and 30), sucrase or invertase (SEQ ID NO: 36), lipase (SEQ ID NO: 39), α-amylases (SEQ ID NO: 42, 45, and 48), laccase (SEQ ID NO: 51), polygalacturonases (SEQ ID NO: 57, 60 and 63), and xylanases (SEQ ID NO: 66, 69, and 72). The biological activities of the gene products encoded by the Aspergillus fumigatus enzyme genes of the invention can be predicted and confirmed by the outcome of their enzymatic actions on substrates commonly encountered by the fungus in its natural habitats or synthetic substrates. Generally, the enzymes of the invention can be used in various methods for modulating the amounts of enzyme substrates and products in a composition. Enzymatically active compositions in various forms as well as antibodies to the enzymes and fragments thereof, are also provided.

[0014] Any or all of these utilities are capable of being developed into a kit for commercialization either as research products or as supplies for industrial uses. The kits may comprise polynucleotides and/or polypeptides corresponding to one or more A. fumigatus enzyme genes of the invention, antibodies, and/or other reagents.

[0015] Various publications and patents are cited hereinbelow, the disclosures of which are incorporated by reference in their entireties.

4. BRIEF DESCRIPTION OF THE DRAWINGS

[0016]FIG. 1: Table 1 lists the sequence identifiers of the genomic and coding sequences of the enzyme genes of the invention, and the amino acid sequences of the encoded polypeptides.

5. DETAILED DESCRIPTION OF THE INVENTION

[0017] Described hereinbelow are the enzyme genes of the invention, their identification, characterization, modification, and methods of use in various industrial processes. All of the publications and patents cited in this section are incorporated by reference in their entireties.

[0018] 5.1. Identification of Aspergillus fumigatus Enzyme Genes

[0019] The nucleotide sequences of Aspergillus fumigatus genomic DNA was obtained by a whole-genome random shotgun DNA sequencing effort. The genomic DNA was prepared from an isolate of A. fumigatus CEA 10 which was isolated from the infected lung tissue of a human aspergillosis patient. The genomic DNA was sheared mechanically into fragments, enzymatically treated to generate blunt ends, and cloned into E. coli pUC 19- and pBR322-based plasmids to form genomic DNA libraries. Average insert sizes of the pUC19-based genomic DNA library clones were about 2 kb and the plasmids were present in high copy numbers in E. coli cells. The other two genomic DNA libraries of pBR322-based clones contain inserts of about 10 kb and about 50 kb respectively. The colonies of genomic clones were transferred robotically to 384-well titre plates; and plasmid DNA templates for dideoxy DNA sequencing reactions were prepared by standard method based on alkaline lysis of cells and isopropanol precipitation of DNA. DNA sequencing reactions were carried out using standard M13 forward and reverse primers and ABI-Prism BigDye terminator chemistry (Applied Biosystems), and analyzed using the capillary array sequencer ABI PRISM 3700 DNA Analyzer (Applied Biosystems). The nucleotide sequences generated were trimmed to discard errors, and assembled to form contigs and scaffolds by the software algorithms developed for sequencing the human genome. For a detailed description of the methodologies of the sequencing reactions and sequence analysis, see Venter et al., 2001, Science 291:1304 and; Myers et al., 2000, Science 287:2196. The set of nucleotide sequence data used in the present invention has an estimated 10×coverage of the A. fumigatus genome.

[0020] The nucleotide sequences were initially annotated by software programs, such as Genescan and Glimmer M (The Institute of Genome Research, Rockville, Md.), which can identify putative coding regions, introns, and splice junctions. Further automated and manual curation of the nucleotide sequences were performed to refine and establish precise characterization of the coding regions and other gene features.

[0021] 5.2. Enzyme Genes

[0022] 5.2.1. Nucleic Acid Molecules of Aspergillus fumigatus

[0023] Described herein are the nucleic acid molecules of the invention that encode enzymes of industrial interest.

[0024] As used herein, the terms “gene” and “recombinant gene” refer to nucleic acid molecules or polynucleotides comprising a nucleotide sequence encoding a polypeptide or a biologically active ribonucleic acid (RNA). The term can further include nucleic acid molecules comprising upstream, downstream, and/or intron nucleotide sequences. The term “open reading frame (ORF),” means a series of nucleotide triplets coding for amino acids without any termination codons and the triplet sequence is translatable into protein using the codon usage information appropriate for a particular organism.

[0025] The term “nucleotide sequence” refers to a heteropolymer of nucleotides, including but not limited to ribonucleotides and deoxyribonucleotides, or the sequence of these nucleotides. The terms “nucleic acid” and “polynucleotide” are also used interchangeably herein to refer to a heteropolymer of nucleotides, which may be unmodified or modified DNA or RNA. For example, polynucleotides can be single-stranded or double-stranded DNA, DNA that is a mixture of single-stranded and double-stranded regions, hybrid molecules comprising DNA and RNA with a mixture of single-stranded and double-stranded regions. In addition, the polynucleotide can be composed of triple-stranded regions comprising DNA, RNA, or both. A polynucleotide can also contain one or modified bases, or DNA or RNA backbones modified for nuclease resistance or other reasons. Generally, nucleic acid segments provided by this invention can be assembled from fragments of the genome and short oligonucleotides, or from a series of oligonucleotides, or from individual nucleotides, to provide a synthetic nucleic acid.

[0026] The term “recombinant,” when used herein to refer to a polypeptide or protein, means that a polypeptide or protein is derived from recombinant (e.g., microbial or mammalian) expression systems. “Microbial” refers to recombinant polypeptides or proteins made in bacterial or fungal expression systems. Polypeptides or proteins expressed in most bacterial systems, e.g., E. coli, will be free of glycosylation modifications; polypeptides or proteins expressed in fungi will be glycosylated.

[0027] The term “expression vehicle or vector” refers to a plasmid, a phage, a virus, an artificial replicating sequence (ARS) or an artificial chromosome for expressing a polypeptide from a nucleotide sequence. An expression vehicle can comprise a transcriptional unit, also referred to as an expression construct, comprising an assembly of (1) a genetic element or elements having a regulatory role in gene expression, for example, promoters or enhancers, (2) a structural or coding sequence which is transcribed into RNA, mRNA and translated into protein, and which is operably linked to the elements of (1); and (3) appropriate transcription initiation and termination sequences. “Operably linked” refers to a link in which the regulatory regions and the DNA sequence to be expressed are joined and positioned in such a way as to permit transcription, as well as translation of the transcripts. Structural units intended for use in fungal or eukaryotic expression systems preferably include a leader or transport sequence enabling extracellular secretion of translated protein by a host cell or targeting of the protein to specific organelle(s). Alternatively, where a recombinant protein is expressed without a leader or transport sequence, it may include an N-terminal methionine residue. This residue may or may not be subsequently cleaved from the expressed recombinant protein to provide a final product.

[0028] The term “recombinant host cells” means cultured cells which comprises a recombinant transcriptional unit, and will express heterologous polypeptides or proteins, and RNA encoded by the DNA segment or synthetic gene in the recombinant transcriptional unit. Such recombinant host cells either have stably integrated a recombinant transcriptional unit into chromosomal DNA or carry stably the recombinant transcriptional unit extrachromosomally. This term also means host cells which have stably integrated a recombinant genetic element or elements having a regulatory role in gene expression, for example, promoters or enhancers. This term include host cells which maintains the recombinant transcriptional unit and/or express the heterologus proteins or RNA transiently. Recombinant expression systems as defined herein will express RNA, polypeptides or proteins endogenous to the cell upon induction of the regulatory elements linked to the endogenous DNA segment or gene to be expressed. The cells can be prokaryotic or eukaryotic.

[0029] The term “polypeptide” refers to the molecule formed by joining amino acids to each other by peptide bonds, and may contain amino acids other than the twenty commonly used gene-encoded amino acids. The term “active polypeptide” refers to those forms of the polypeptide which retain the enzymatic, biologic and/or immunologic activities of any naturally occurring polypeptide. The term “naturally occurring polypeptide” refers to polypeptides produced by cells that have not been genetically engineered and specifically contemplates various polypeptides arising from post-translational modifications of the polypeptide including, but not limited to, proteolytic processing, acetylation, carboxylation, glycosylation, phosphorylation, lipidation and acylation.

[0030] The term “isolated” as used herein refers to a nucleic acid or polypeptide separated from at least one macromolecular component (e.g., nucleic acid or polypeptide) present with the nucleic acid or polypeptide in its natural source. In one embodiment, the polynucleotide or polypeptide constitutes at least 95% by weight, more preferably at least 99.8% by weight, of the indicated biological macromolecules present (but water, buffers, and other small molecules, especially molecules having a molecular weight of less than 1000 daltons, can be present).

[0031] Encompassed by the present invention are genomic nucleotide sequences and coding sequences of genes that encode enzymes of Aspergillus fumigatus of industrial interest. Accordingly, in one embodiment, SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, and 71 are provided each of which identifies a nucleotide sequence of the opening reading frame (ORF) of an identified enzyme gene. In another embodiment, the genomic sequences of the enzyme genes identified by SEQ ID NO: 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70 are provided.

[0032] The DNA sequences of the invention were generated by sequencing reactions and may contain minor errors which may exist as misidentified nucleotides, insertions, and/or deletions. However, such minor errors, if present, should not disturb the identification of the sequences as a gene of A. fumigatus that encodes an enzyme of industrial interest, and are specifically encompassed within the scope of the invention.

[0033] The enzyme genes listed in Table 1 can be obtained using cloning methods well known to those of skill in the art, and include but are not limited to the use of appropriate probes to detect the genes within an appropriate cDNA or gDNA (genomic DNA) library (See, for example, Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratories,). Probes for the sequences identified herein can be synthesized based on the DNA sequences disclosed herein in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70.

[0034] As used herein, “enzyme gene” refers to (a) a gene comprising at least one of the nucleotide sequences and/or fragments thereof that are set forth in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70; (b) any nucleotide sequence or fragment thereof that encodes the amino acid sequence that are set forth in SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72; (c) any nucleotide sequence that hybridizes to the complement of the nucleotide sequences set forth in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70 under medium stringency conditions, e.g., hybridization to filter-bound DNA in 6×sodium chloride/sodium citrate (SSC) at about 45° C. followed by one or more washes in 0.2×SSC/0.1% SDS at about 50 to 65° C., or under highly stringent conditions, e.g., hybridization to filter-bound nucleic acid in 6×SSC at about 45° C. followed by one or more washes in 0.1×SSC/0.2% SDS at about 68° C., or under other hybridization conditions which are apparent to those of skill in the art (see, for example, Ausubel, F. M. et al., eds., 1989, Current Protocols in Molecular Biology, Vol. 1, Green Publishing Associates, Inc. and John Wiley & Sons, Inc., New York, at pp. 6.3.1-6.3.6 and 2.10.3). Preferably, the polynucleotides that hybridize to the complements of the DNA sequences disclosed herein encode gene products, e.g., gene products that are functionally equivalent to a gene product encoded by one of the enzyme genes or fragments thereof.

[0035] As described above, enzyme gene sequences include not only degenerate nucleotide sequences that encode the amino acid sequences of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, but also degenerate nucleotide sequences that when translated in organisms other than Aspergillus fumigatus, would yield a polypeptide comprising one of the amino acid sequences of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, or a fragment thereof. One of skill in the art would know how to select the appropriate codons or modify the nucleotide sequences of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67 and 70, when using the enzyme gene sequences in A. fumigatus or in other organisms. For example, in Candida albicans, the codon CTG encodes a serine residue instead of leucine residue.

[0036] Moreover, the term “enzyme gene” encompasses genes that are naturally occurring in closely related Aspergillus species or variant strains of A. fumigatus, that share extensive nucleotide sequence homology with A. fumigatus genes having one of the DNA sequences that are set forth in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70. It is contemplated that methods for identification of the enzyme genes of A. fumigatus can also be applied to orthologs of the same genes in A. fumigatus and other fungal species, including but not limited to other Aspergillus species.

[0037] In another embodiment, the invention also encompasses the following polynucleotides, host cells expressing such polynucleotides and the expression products of such nucleotides: (a) polynucleotides that encode portions of enzyme gene product that corresponds to its active sites and/or functional domains, and the polypeptide products encoded by such nucleotide sequences, and in which, in the case of secreted gene products, such domains include, but are not limited to signal sequences; and (b) polynucleotides that encode fusion proteins containing an enzyme gene product or one of its active sites and/or domains fused to another polypeptide.

[0038] The invention also includes polynucleotides, preferably DNA molecules, that hybridize to, and are therefore the complements of, the DNA sequences of the enzyme gene sequences. Such hybridization conditions can be highly stringent or less highly stringent, as described above and known in the art. The nucleic acid molecules of the invention that hybridize to the above described DNA sequences include oligodeoxynucleotides (“oligos”) which hybridize to the enzyme gene under highly stringent or stringent conditions. In general, for oligos between 14 and 70 nucleotides in length the melting temperature (Tm) is calculated using the formula:

Tm(° C.)=81.5+16.6(log[monovalent cations (molar)]+0.41(% G+C)−(500/N)

[0039] where N is the length of the probe. If the hybridization is carried out in a solution containing formamide, the melting temperature may be calculated using the equation:

Tm(° C.)=81.5+16.6(log[monovalent cations (molar)])+0.41(% G+C)−(0.61)(% formamide)−(500/N).

[0040] where N is the length of the probe. In general, hybridization is carried out at about 20-25 degrees below Tm (for DNA-DNA hybrids) or about 10-15 degrees below Tm (for RNA-DNA hybrids). Other exemplary highly stringent conditions may refer, e.g., to washing in 6×SSC/0.05% sodium pyrophosphate at 37° C. (for 14-base oligos), 48° C. (for 17-base oligos), 55° C. (for 20-base oligos), and 60° C. (for 23-base oligos).

[0041] In another embodiment of the invention, RNA capable of encoding enzyme gene protein sequences are provided. Such RNA molecules can be chemically synthesized using, for example, synthesizers. See, for example, the techniques described in Oligonucleotide Synthesis, 1984, Gait, M. J. ed., IRL Press, Oxford, which is incorporated by reference herein in its entirety. Alternatively, the RNA molecules can be generated biologically by transcription of one of the DNA molecules described above.

[0042] In various embodiments, these nucleic acid molecules, DNA or RNA, can encode or act as enzyme gene antisense molecules, useful, for example, in enzyme gene regulation and/or as antisense primers in amplification reactions of enzyme gene nucleotide sequences. Further, such sequences can be used as part of ribozyme and/or triple helix sequences, also useful for enzyme gene regulation. Still further, such molecules can be used as components of diagnostic methods whereby the presence of the fungus can be detected. The uses of these nucleic acid molecules are discussed in detail below.

[0043] Fragments of the enzyme genes of the invention can be at least 16 nucleotides in length. In alternative embodiments, the fragments can be at least about 20, 30, 40, 50, 60, 70, 80, 90, 100, 200, 300, 400, 500, 1000, 1500, 2000, 2500, 3000, 3500, 4000, 4500, 5000 or more contiguous nucleotides in length. Alternatively, the fragments can comprise nucleotide sequences that encode about 10, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 900, 1000 or more contiguous amino acid residues of the target gene products. Fragments of the enzyme genes of the invention can also refer to exons or introns of the above described nucleic acid molecules, as well as portions of the coding regions of such nucleic acid molecules that encode functional domains such as signal sequences and active site(s). Many such fragments can be used as nucleic acid probes for the identification of other homologous genes of A. fumigatus in the same enzyme family.

[0044] In another embodiment, the present invention is directed toward the regulatory regions that are found upstream and downstream of the coding sequences disclosed herein, which are readily determined and isolated from the genomic sequences provided herein. Included within such regulatory regions are, inter alia, promoter sequences, upstream activator sequences, as well as binding sites for regulatory proteins that modulate the expression of the genes identified herein.

[0045] The nucleotide sequences of enzyme genes of Aspergillus fumigatus can be used to produce recombinant enzymes, and fragments thereof. The recombinantly produced polypeptide and fragments thereof can be used individually, or in combination as an immunogen or a subunit vaccine to elicit a protective immune response in animals or subjects at high risk of developing a clinical condition, such as those that are under continual exposure of high levels of Aspergillus fumigatus conidia.

[0046] The nucleotide sequences of the invention can be used as genetic markers and/or sequence markers to aid the development of a genetic, physical, or sequence map of the Aspergillus fumigatus genome. The nucleotide sequences and corresponding gene products of the invention can also be used to detect the presence of A. fumigatus. Hybridization and antibody-based methods well known in the art can be used to determine the presence and concentration of the nucleotide sequences and corresponding gene products of the invention.

[0047] The nucleotide sequences can also be used for identifying inhibitors of the enzymes which may have therapeutic effects, given the fact that the enzymes may play a role in the invasion of a host during an infection.

[0048] 5.2.2. Homologous Enzyme Genes

[0049] In another embodiment, in addition to the nucleotide sequences of Aspergillus fumigatus described above, homologs or orthologs of the enzyme genes of the invention as can be present in A. fumigatus and other fungal species are also encompassed. Particularly preferred are homologs or orthologs in filamentous fungi and yeasts. These enzyme genes can be identified and isolated by molecular biological techniques well known in the art.

[0050] “Fungi” as used herein includes the phyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota (as defined by Hawksworth et al., In, Ainsworth and Bisby's Dictionary of The Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UK) as well as the Oomycota (as cited in Hawksworth et al., 1995, supra, page 171) and all mitosporic fungi (Hawksworth et al., 1995, supra). Representative groups of Ascomycota include, e.g., Neurospora, Eupenicillium (i.e., Penicillium), Emericella and Eurotium (i.e., Aspergillus), and the true yeasts listed above. Examples of Basidiomycota include mushrooms, rusts, and smuts. Representative groups of Chytridiomycota include, e.g., Allomyces, Blastocladiella, Coelomomyces, and aquatic fungi. Representative groups of Oomycota include, e.g., Saprolegniomycetous aquatic fungi (water molds) such as Achlya. Examples of mitosporic fungi include Aspergillus, Penicillium, Candida, and Altemaria. Representative groups of Zygomycota include, e.g., Rhizopus and Mucor.

[0051] “Filamentous fungi” include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al., 1995, supra). The filamentous fingi are characterized by a vegetative mycelium composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth is by hyphal elongation and carbon catabolism is obligately aerobic. In contrast, vegetative growth by yeasts such as Saccharomyces cerevisiae is by budding of a unicellular thallus and carbon catabolism may be fermentative.

[0052] “Yeast” as used herein includes ascosporogenous yeast (Endomycetales), basidiosporogenous yeast, and yeast belonging to the Fungi Imperfecti (Blastomycetes). The ascosporogenous yeasts are divided into the families Spermophthoraceae and Saccharomycetaceae. The latter is comprised of four subfamilies, Schizosaccharomycoideae (e.g., genus Schizosaccharomyces), Nadsonioideae, Lipomycoideae, and Saccharomycoideae (e.g., genera Pichia, Kluyveromyces and Saccharomyces). The basidiosporogenous yeasts include the genera Leucosporidim, Rhodosporidium, Sporidiobolus, Filobasidium, and Filobasidiella. Yeast belonging to the Fungi Imperfecti are divided into two families, Sporobolomycetaceae (e.g., genera Sorobolomyces and Bullera) and Cryptococcaceae (e.g., genus Candida). For the purposes of this invention, yeast shall be defined as described in Biology and Activities of Yeast (Skinner, F. A., Passmore, S. M., ana Davenport, R. R., eds, Soc. App. Bacteriol. Symposium Series No. 9, 1980). The biology of yeast and manipulation of yeast genetics are well known in the art (see, e.g., Biochemistry and Genetics of Yeast, Bacil, M., Horecker, B. J., and Stopani, A. O. M., editors, 2nd edition, 1987; The Yeasts, Rose, A. H., and Harrison, J. S., editors, 2nd edition, 1987; and The Molecular Biology of the Yeast Saccharomyces, Strathem et al., editors, 1981).

[0053] Accordingly, the present invention provides fungal nucleotide sequences that are hybridizable to the polynucleotides of the enzyme genes. In one embodiment, the present invention encompasses an isolated nucleic acid comprising a nucleotide sequence that is at least 50% identical to a nucleotide sequence selected from the group consisting of SEQ ID NO.: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70.

[0054] In another embodiment, the present invention encompasses an isolated nucleic acid comprising a fungal nucleotide sequence that hybridizes under medium stringency conditions to a second nucleic acid that consists of a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70.

[0055] In yet another embodiment, the present invention includes an isolated nucleic acid comprising a fungal nucleotide sequence that encodes a polypeptide the amino acid sequence of which is at least 50% identical to an amino acid sequence selected from the group consisting of SEQ ID No. 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72.

[0056] The nucleotide sequences of the invention still further include fungal nucleotide sequences that have at least 40%,45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or more nucleotide sequence identity to the nucleotide sequences set forth in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, 70, 73, 76, 79.

[0057] The nucleotide sequences of the invention also include fungal nucleotide sequences that encode polypeptides having at least 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%,70%, 75%, 80%, 85%, 90%, 95%, 96%,97%, 98%, 99% or higher amino acid sequence identity or similarity to the amino acid sequences set forth in SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72.

[0058] To determine the percent identity of two amino acid sequences or of two nucleotide sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of a first amino acid or nucleotide sequence for optimal alignment with a second amino acid or nucleotide sequence). See, for example, the method of Huang and Miller (1991, Adv. Appl. Math, 12:373-381). The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % identity=number of identical overlapping positions/total number of positions×100). In one embodiment, the two sequences are substantially similar in length.

[0059] The determination of percent identity between two sequences can also be accomplished using a mathematical algorithm. A preferred, non-limiting example of a mathematical algorithm utilized for the comparison of two sequences is the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. U.S.A. 87:2264-2268, modified as in Karlin and Altschul (1993) Proc. Natl. Acad. Sci. U.S.A. 90:5873-5877. Such an algorithm is incorporated into the NBLAST and XBLAST programs of Altschul et al., 1990, J. Mol. Biol. 215:403-0. BLAST nucleotide searches can be performed with the NBLAST nucleotide program parameters set, e.g., for score=100, wordlength=12 to obtain nucleotide sequences homologous to a nucleic acid molecules of the present invention. BLAST protein searches can be performed with the XBLAST program parameters set, e.g., to score-50, wordlength=3 to obtain amino acid sequences homologous to a protein molecule of the present invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., 1997, Nucleic Acids Res. 25:3389-3402. Alternatively, PSI-BLAST can be used to perform an iterated search which detects distant relationships between molecules (Id.). When utilizing BLAST, Gapped BLAST, and PSI-Blast programs, the default parameters of the respective programs (e.g., of XBLAST and NBLAST) can be used (see, e.g., http://www.ncbi.nlm.nih.gov). Another preferred, non-limiting example of a mathematical algorithm utilized for the comparison of sequences is the algorithm of Myers and Miller, (1988) CABIOS 4:11-17. Such an algorithm is incorporated in the ALIGN program (version 2.0) which is part of the GCG sequence alignment software package. When utilizing the ALIGN program for comparing amino acid sequences, a PAM120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used.

[0060] Although the nucleotide sequences and amino acid sequences of homologs or orthologs of many enzyme genes in Saccharomyces cerevisiae is published, as well as those homologs or orthologs of enzyme genes in Candida albicans which may be available as database version 6 assembled by the Candida albicans Sequencing Project and is accessible by internet at the web sites of Stanford University and University of Minnesota (See http://www-sequence.stanford.edu:8080/and http://alces.med.umn.edu/Candida.html), uses of many of such genes in S. cerevisiae or in C. albicans as industrial enzymes are not known and are thus specifically provided by the invention.

[0061] In addition, the genuses of isolated nucleic acid molecules provided in various embodiments of the invention does not comprise the nucleotide sequence of Genbank Accession No. D63338 encoding a tannase of Aspergillus oryzae, Genbank Accession No. AB022429 encoding a cellobiohydrolase II of Acremonium celluloticus Y-94, Genbank Accession No. AE004826 encoding an enzyme of Pseudomonas aeruginosa, Genbank Accession No. U56240 encoding a glucose oxidase of Talaromyces flavus, Genbank Accession No. AF012277 encoding a glucose oxidase of Penicillium amagasakiense, Genbank Accession No. U59804 encoding a phytase of Aspergillus fumigatus, Genbank Accession No. S37150 encoding a beta-galactosidase of Aspergillus niger, Genbank Accession No. A00968 encoding a beta-galactosidase of Aspergillus niger, Genbank Accession No. AJ304803 encoding a glucoamylase of Talaromyces emersonii, Genbank Accession No. AJ289046 encoding a fructosyltransferase of Aspergillus sydowii, Genbank Accession No. A84689 encoding a protein product of Aspergillus tubingensis, Genbank Accession No. X12726 encoding an alpha-pre-amylase of Aspergillus oryzae, Genbank Accession No. AB008370 encoding an acid-stable alpha-amylase of Aspergillus kawachii, Genbank Accession No. AF208225 encoding an alpha-anylase Amy A of Aspergillus nidulans, Genbank Accession No. AF104823 of a gene product of Aspergillus fumigatus, Genbank Accession No. 010460 encoding a glucoarnylase Aspergillus shirousami, Genbank Accession No. AF052061 encoding a polygalacturonase of Ophiostoma novo-ulmi, Genbank Accession No. X58892 encoding a polygalacturonase of Aspergillus niger, Genbank Accession No. Y18805 encoding an endo-polygalacturonase B of Aspergillus niger, Genbank Accession No. AB003085 encoding XynG1 of Aspergillus oryzae, Genbank Accession No. AB044941 encoding a xylanase G2 of Aspergillus oryzae, and Genbank Accession No. AB035540 encoding a xylanase A of Penicillium sp.40. The gene products encoded by the foregoing Genbank nucleotide sequences are also not included in the genuses of gene products contemplated in the present invention.

[0062] To isolate homologous enzyme genes, the Aspergillus fumigatus enzyme gene sequence described above can be labeled and used to screen a cDNA library constructed from mRNA obtained from the organism of interest, including but not limited to A. fumigatus. Accordingly, nucleic acid probes, preferably detectably labeled, consisting of any one of the nucleotide sequences of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70 are encompassed. Hybridization conditions should be of a lower stringency when the cDNA library was derived from an organism different from the type of organism from which the labeled sequence was derived. cDNA screening can also identify clones derived from alternatively spliced transcripts in the same or different species. Alternatively, the labeled probe can be used to screen a genomic library derived from the organism of interest, again, using appropriately stringent conditions. Low stringency conditions will be well known to those of skill in the art, and will vary predictably depending on the specific organisms from which the library and the labeled sequences are derived. For guidance regarding such conditions see, for example, Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press, N.Y.; and Ausubel et al., 1989, Current Protocols in Molecular Biology, (Green Publishing Associates and Wiley Interscience, N.Y.).

[0063] Further, a homologous enzyme gene sequence can be isolated by performing a polymerase chain reaction (PCR) using two degenerate oligonucleotide primer pools designed on the basis of amino acid sequences within the enzyme gene of interest. The template for the reaction can be cDNA obtained by reverse transcription of mRNA prepared from the organism of interest. The PCR product can be subcloned and sequenced to ensure that the amplified sequences represent the sequences of a homologous enzyme gene sequence.

[0064] The PCR fragment can then be used to isolate a full length cDNA clone by a variety of methods well known to those of ordinary skill in the art. Alternatively, the labeled fragment can be used to screen a genomic library.

[0065] PCR technology can also be utilized to isolate full length cDNA sequences.

[0066] For example, RNA can be isolated, following standard procedures, from an organism of interest. A reverse transcription reaction can be performed on the RNA using an oligonucleotide primer specific for the most 5′ end of the amplified fragment for the priming of first strand synthesis. The resulting RNA/DNA hybrid can then be “tailed” with guanines using a standard terminal transferase reaction, the hybrid can be digested with RNAase H, and second strand synthesis can then be primed with a poly-C primer. Thus, cDNA sequences upstream of the amplified fragment can easily be isolated. For a review of cloning strategies which can be used, see e.g., Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual, Cold Springs Harbor Press, N.Y.; and Ausubel et al., 1989, Current Protocols in Molecular Biology, (Green Publishing Associates and Wiley Interscience, N.Y.).

[0067] Additionally, an expression library can be constructed utilizing DNA isolated from or cDNA synthesized from the organism of interest. In this manner, gene products made by the homologous enzyme gene can be expressed and screened using standard antibody screening techniques in conjunction with antibodies raised against the Aspergillus fumigatus gene product, as described, below. (For screening techniques, see, for example, Harlow, E. and Lane, eds., 1988, “Antibodies: A Laboratory Manual,” Cold Spring Harbor Press, Cold Spring Harbor). Library clones detected via their reaction with such labeled antibodies can be purified and subjected to sequence analysis by well known methods.

[0068] Alternatively, a database may be searched to determine whether any amino acid sequences or nucleotide sequences display a certain level of homology or sequence identity with respect to the enzyme genes or enzymes. A variety of such databases are available to those skilled in the art, including GenBank and GenSeq. In various embodiments, the databases are screened to identify nucleic acids with at least 97%, at least 95%, at least 90%, at least 85%, at least 80%, at least 70%, at least 60%, at least 50%, or at least 40% nucleotide sequence identity to an enzyme gene sequence, or a portion thereof. In other embodiments, the databases are screened to identify polypeptides having at least 99%, at least 95%, at least 90%, at least 85%, at least 80%, at least 70%, at least 60%, at least 50%, at least 40% or at least 25% amino acid identity or similarity to a polypeptide encoded by the enzyme genes of the invention.

[0069] Alternatively, functionally homologous enzyme sequences or polypeptides may be identified by creating mutations by removing or altering the function of an enzyme gene. Having mutants in the genes of one fungal species offers a method to identify functionally similar genes or related genes (orthologs) in another species, or functionally similar genes in the same species (paralogs), by use of a functional complementation test.

[0070] A library of gene or cDNA copies of messenger RNA of genes can be made from a species of interest, and the library cloned into a vector permitting expression of the genes in A. fumigatus. Such a library is referred to as a “heterologous library.” Transformation of the heterologous library into a defined mutant of A. fumigatus that is functionally deficient with respect to the identified enzyme gene, and screening or selecting for a gene in the heterologous library that restores phenotypic function in whole or in part of the mutational defect is said to be “heterologous functional complementation”. In this example, the method permits identification of gene in the species of interest that are functionally related to the mutated gene in A. fumigatus. Inherent in this functional-complementation method, is the ability to restore gene function without the requirement for sequence similarity of nucleic acids or polypeptides; that is, this method permits interspecific identification of genes with conserved biological function, even where sequence similarity comparisons fail to reveal or suggest such conservation.

[0071] 5.2.3. Mutagenesis of A. fumigatus Enzyme Genes

[0072] In another embodiment of the invention, the Aspergillus fumigatus enzyme gene sequences can be used in developing modified or novel enzymes that exhibit particularly desirable chemical and/or physical characteristics. Because of the apparent relatedness of the amino acid sequences among the enzymes of Aspergillus fumigatus and other filamentous fungi, the structure of an enzyme of another fungus can be used to predict the structure of the A. fumigatus enzyme, and aid in the rational modification of the A. fumigatus enzyme for useful and superior properties. The sequences provided by the present invention can also be used as starting materials for the rational modification or design of novel enzymes with characteristics that enable the enzymes to perform better in demanding processes.

[0073] In one aspect, the sequence, structural, and functional information of the various members of a single enzyme family of A. fumigatus can be compiled and compared. The invention provides the sequences of three members of each of the following enzyme families: glucose oxidases, xylanases, α-amylases, glucoamylases, and polygalacturonases. The results can be used to generate a structural model for the A. fumigatus enzymes including a determination of the active sites, substrate binding sites, etc. with the aid of computers (Bugg et al., Scientific American, December:92-98 (1993); West et al., TIPS, 16:67-74 (1995); Dunbrack et al., Folding & Design, 2:2742 (1997)). The nucleotide sequences of the enzyme genes can be used to produce recombinantly large amounts of the enzymes sufficient to obtain crystals of the enzymes. Methods known in the art for obtaining crystals and X-ray crystallography can be applied to generate a 3-D structure of an enzyme of the invention. In another aspect, the sequence, structural, and functional information of other homologous enzyme gene sequences can be combined and superimposed to assist in the modeling and design processes. Computer analysis may be performed with one or more of the computer programs including: QUANTA, CHARMM, FlexX, INSIGHT, SYBYL, MACROMODEL and ICM.

[0074] In particular, the invention encompasses the uses of nucleotide sequences of the invention to design or to generate modified enzymes which possess temperature optima that are either higher or lower than that of the wild type A. fumigatus enzyme, pH optima that are either higher or lower than that of the wild type A. fumigatus enzyme, specific activities that are higher than that of the wild type A. fumigatus enzyme, or a longer half-life than the wild type A. fumigatus enzyme under a particular process condition, such as the presence of detergents. The enzyme gene nucleotide sequences can be altered by random and site-directed mutagenesis techniques or directed molecular evolution techniques, such as but not limited to the methods described in Arnold (1993, Curr. Opinion Biotechnol. 4:450-455), oligonucleotide-directed mutagenesis (Reidhaar-Olson et al., 1988, Science 241:53-57), chemical mutagenesis (Eckert et al., Mutat. Res. (1987) 178:1-10), site-directed mutagenesis (Kunkel (1985) Proc. Natl. Acad. Sci. USA 82:488492; Oliphant et al., (1986) Gene 44:177-183), error prone PCR (Caldwell and Joyce, 1992, PCR Methods Applic. 2:28-33), cassette mutagenesis (Arkin et al., Proc. Natl. Acad. Sci. USA, 1992, 89:7871-7815), DNA shuffling methods as described in Stemmer et al., 1994, Proc. Natl. Acad. Sci. USA, 91:10747-10751 and in U.S. Pat. Nos. 5,605,793; 6,117,679; and 6,132,970, and the methods as described in U.S. Pat. Nos. 5,939,250, 5,965,408, 6,171,820. In certain embodiments, nucleotide sequences of other related enzyme genes that encodes similar domains, structural motifs, or active sites, or that aligns with a portion of the enzyme gene of the invention with mismatches or imperfect matches, can be used in the mutagenesis process to generate diversity of sequences. It should be understood that for each mutagenesis step in some of the techniques mentioned above, a number of iterative cycles of any or all of the steps may be performed to optimize the diversity of sequences. The above-described methods can be used in combination in any desired order. In many instances, the methods result in a pool of mutant nucleotide sequences or a pool of recombinant host cells comprising mutant nucleotide sequences. The nucleotide sequences or host cells expressing a modified enzyme with the desired characteristics can be identified by screening with one or more enzymatic assays that are well known in the art. The assays maybe carried out under conditions that select for enzymes possessing the desired physical or chemical characteristics. The mutations in the nucleotide sequence can be determined by sequencing the enzyme gene in the clones.

[0075] 5.2.4. Vectors, Expression Constructs, and Recombinant Host Cells

[0076] In another embodiment, the invention also encompasses (a) nucleic acid vectors that comprise a nucleotide sequence comprising any of the foregoing sequences of the enzyme genes and/or their complements (including antisense molecules); (b) expression constructs that comprise a nucleotide sequence comprising any of the foregoing coding sequences of the enzyme genes operably linked with a regulatory element that directs the expression of the coding sequences; and (c) recombinant host cells that comprise any of the foregoing sequences of the enzyme gene, including coding regions operably linked with a regulatory element that directs the expression of the coding sequences in the host cells.

[0077] Recombinant DNA methods which are well known to those skilled in the art can be used to construct vectors comprising coding sequences of the enzyme genes, and appropriate transcriptional/translational control signals. The various sequences may be joined in accordance with known techniques, such as restriction, joining complementary restriction sites and ligating, blunt ending by filling in overhangs and blunt ligation, Bal31 treatment, primer repair, in vitro mutagenesis, or the like. Polylinkers and adapters may be employed, when appropriate, and introduced or removed by known techniques to allow for ease of assembly of the DNA vectors and expression constructs. These methods may also include in vivo recombination/genetic recombination. At each stage of the manipulation of the enzyme gene sequences, the fragment(s) may be cloned, analyzed by restriction enzyme, sequencing or hybridization, or the like. A large number of vectors are available for cloning and genetic manipulation. Normally, cloning can be performed in E. coli. See, for example, the techniques described in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Press, Cold Spring Harbor, N.Y.; Ausubel, 1989, supra; Methods in Enzymology: Guide to Molecular Cloning Techniques, Academic Press, Berger, S. L. and A. R. Kimmel eds., 1987; Pla et al., Yeast 12:1677-1702 (1996); Kinghom and Unkles in Aspergillus, ed. by J. E. Smith, Plenum Press, New York, 1994, Chapter 4, p.65-100.

[0078] In various embodiments of the invention, nucleic acid vectors that comprise an enzyme gene sequence of the invention, may further comprise replication functions that enable the transfer, maintenance and propagation of the vectors in one or more species of host cells, including but not limited to E. coli cells, filamentous fungal cells, yeast cells, and Bacillus cells. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vectors may be linear or closed circular plasmids, cosmid, or phagemids. The vector may be an autonomously replicating vector, i.e., a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means for assuring self-replication. Alternatively, the vector may be one which, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. The vector system may be a single vector or plasmid or two or more vectors or plasmids which together contain the total nucleic acid to be introduced into the genome of the host cell, or a transposon.

[0079] A expression construct of the invention comprises a promoter, a nucleotide sequence encoding for an enzyme gene, a transcription termination sequence, and optionally, a selectable marker. If the expression host that is used to produce the polypeptide or peptide does not use the universal genetic code, gene products of the enzyme genes having the amino acid sequences of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, may be encoded by nucleotide sequences that conform to the known codon usage in the host. One of skill in the art would know the modifications that are necessary to accommodate for a difference in codon usage. When an expression construct comprising the enzyme gene sequence of the invention is introduced into a host cell by transformation, the enzyme gene sequence is transcribed and translated to produce the corresponding polypeptide, and an increase in the enzyme activity can be demonstrated functionally. Accordingly, the present invention also relates to methods for producing an polypeptide of the present invention comprising (a) cultivating a host cell under conditions conducive to expression of the polypeptide; and (b) recovering the polypeptide.

[0080] Any method known in the art for introducing the enzyme gene sequences of the invention into a host cell can be used, including those described hereinbelow. Fungal cells may be transformed by a process involving protoplast formation, transformation of the protoplasts, and regeneration of the cell wall. Suitable procedures for transformation of Aspergillus host cells are described in EP 238 023 and Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81:1470-1474.

[0081] A suitable method of transforming Fusarium species is described by Malardier et al., 1989, Gene 78:147-156. Other methods may include using co-transformation, lithium acetate treatment of conidia, electroporation (Ward et al., 1989, Exp. Mycol. 13:289-293), and microprojectiles (Armaleo et al., 1990, Curr. Genet. 17:97-103). See also Fincham (1989, Microbiol. Rev. 53:148-170), and May (1992, Fungal Technology, in Applied Molecular Genetics of Filamentous Fungi, Blackie Press, Glasgow). Yeast may be transformed using the procedures described by Becker and Guarente, In Abelson, J. N. and Simon, M. I., editors, Guide to Yeast Genetics and Molecular Biology, Methods in Enzymology, Volume 194, pp 182-187, Academic Press, Inc., New York; Ito et al., 1983, Journal of Bacteriol. 153:163; and Hinnen et al., 1978, Proc. Natl. Acad. Sci. USA 75:1920.

[0082] The isolation of the enzyme gene sequences of the invention enables the economical production of the respective enzymes on an industrial scale, via the application of techniques known in the art such as gene amplification, the exchange of regulatory elements such as promoters, secretory signals, or combinations thereof. Accordingly, the present invention also comprises an expression host capable of the efficient expression of high levels of peptides or proteins having the enzyme activity of interest and, if desired depending on the application, the expression of additional enzymes as well. Preferably, the enzymes are secreted by the expression host.

[0083] For a majority of the industrial applications, the enzymes of the invention are produced by a fungal cell. Preferably, the expression host cell is a filamentous fungal cell which has been used in large scale industrial fermentation. In many instances, the most preferred are host cells that are approved by regulatory authorities, such as the United States Food and Drug Administration, for production of food substances. For example, GRAS (generally-regarded-as-safe) organisms are preferred. In addition, a host cell strain can be chosen which modulates the expression of the inserted sequences, or modifies and processes the gene product in the specific fashion desired. Such modifications (e.g., glycosylation) and processing (e.g., cleavage) of protein products can be important for the function of the protein. Different host cells have characteristic and specific mechanisms for the post-translational processing and modification of proteins. Appropriate cell lines or host systems can be chosen to ensure the correct modification and processing of the foreign protein expressed. Preferably, an expression host is selected which is capable of the efficient secretion of their endogenous proteins. A host cell may also be chosen for deficiencies in extracellular protease activities since the secreted enzyme may be degraded in the culture medium.

[0084] Preferred expression hosts include filamentous fungi selected from the genera Acremonium, Aspergillus, Fusarium, Humicola, Myceliophthora, Neurospora, Thielavia, Tolypocladium, Trichodenna, Mucor and Penicillium. In a most preferred embodiment, industrial strains of Aspergillus, especially A. niger, A. ficuum, A. awamori, A. foetidus, A. japonicus and A. oryzae, can be used. Alternatively, Trichodenna reesei, or Mucor miehei, may be used. The fungal host cell can also be a yeast cell of a species of Candida, Kluyveromyces, Saccharomyces, Schizosaccharomyces, Pichia, or Yarrowia. In a preferred embodiment, the yeast host cell is a Saccharomyces cerevisiae, a Saccharomyces carlsbergensis, a Saccharomyces diastaticus, a Saccharomyces douglasii, a Saccharomyces kluyveri, a Saccharomyces norbensis, or a Saccharomyces ovifomis cell, a Kluyveromyces lactis cell, or a Yarrowia lipolytica cell.

[0085] As used herein, regulatory elements include but are not limited to inducible and non-inducible promoters, enhancers, operators and other elements known to those skilled in the art that enable and regulate expression. Generally, the region 5′ to the open reading frame in the enzyme gene sequence of the invention comprises the transcriptional initiation regulatory region (or promoter) which can be used for expression in fungi. Alternatively, any regulatory region functional in the host may be employed. In preferred embodiments, promoters of genes which are homologous to the enzyme gene sequence to be expressed may be used. Promoters of genes of the expression host are most preferred. For expression in fungal cells, fungal regulatory elements may include those associated with alcohol dehydrogenases (adhA, alcA, alcC; inducible by ethanol), isopenicillin N synthetase (pcbc), pyr4, pyrG, glyceraldehyde-3-phosphate dehydrogenase (gpda, constitutive); mprA (aspartyl protease of Mucor miehel); and promoters isolated from genes involved in carbohydrate metabolism such as amylases (amyA, amy(taka), inducible by starch); glucoamylases (glaA, inducible by maltose, starch, maltodextrin). For further examples, see Van den Hondel et al., Heterologous gene expression infilamentous fungi, chapter 18, pp. 396-428 in More Gene Manipulations in Fungi, Academic Press, 1991. Particularly preferred promoters for use in filamentous fungal host cells are the TAKA amylase, NA2-tpi (a hybrid of the promoters from the genes encoding Aspergillus niger neutral α-amylase and Aspergillus oryzae triose phosphate isomerase), and glaA promoters. In a yeast host, useful promoters are obtained from the Saccharomyces cerevisiae enolase (ENO-1) gene, the S. cerevisiae galactokinase gene (GAL1), the S. cerevisiae alcohol dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase genes (ADH2/GAP), and the S. cerevisiae 3-phosphoglycerate kinase gene, and genes relating to amino acid metabolism (e.g. MET genes) and the acid phosphatase gene. Other useful promoters for yeast host cells include the yeast mating pheromone responsive promoters (e.g. STE2 and STE3), the AOX1 system for Pichia pastoris, the phosphate-responsive promoters (e.g. PH05), and those described by Romanos et al., 1992, Yeast 8:423-488.

[0086] In certain instances, specific initiation signals may also be required for efficient translation of inserted enzyme gene coding sequences. These signals include the ATG initiation codon and adjacent sequences. In cases where an entire enzyme gene, including its own initiation codon and adjacent sequences, is inserted into the appropriate expression vector, no additional translational control signals are needed. However, in cases where only a portion of the enzyme gene coding sequence is inserted, or the Aspergillus fumigatus signals are not efficient in a particular host cell, exogenous translational control signals, including, the ATG initiation codon, may be provided. Furthermore, the initiation codon must be in phase with the reading frame of the desired coding sequence to ensure proper translation of the entire sequence. These exogenous translational control signals and initiation codons can be of a variety of origins, both natural and synthetic. For example, (C/T)CA(C/A)(C/A)ATG, may be used with many filamentous fungi (Gurr et al., 1988, in Gene Structure in Eukaryotic Microbes, ed. by Kinghom, Society of General Microbiology Special Publication, 23:93-139, IRL Press, Oxford.

[0087] The expression construct of the invention may also comprise a peptide sequence which provides for secretion of the expressed peptide or protein from the host. Various signal sequences (also referred to as leader sequences) may be used. Preferred signal sequences include signal sequences of the homologous enzyme genes of the expression host. The signal peptide coding region may be obtained from a glucoamylase or an amylase gene from an Aspergillus species, a lipase or proteinase gene from a Rhizomucor species, the gene for the α-factor from Saccharomyces cerevisiae, an amylase or a protease gene from a Bacillus species, or the calf preprochymosin gene. However, any signal peptide coding region capable of directing the expressed enzyme into the secretory pathway of a host cell of choice may be used in the present invention. The nucleotide sequence encoding the signal sequence maybe joined directly through the sequence encoding the processing signal to the sequence encoding the desired protein, or through a short linker, usually fewer than ten codons. The short linker may also contain a protease cleavage site, such as but not limited to the Kex2 or factor Xa cleavage sites.

[0088] A transcriptional termination regulatory region is operably linked to the 3′ terminus of the nucleic acid sequence encoding the polypeptide. A polyadenylation sequence may also be included in this region. Any terminator which is functional in the host cell of choice may be used in the present invention. The terminator sequence may be from any gene of Aspergillus fumigatus including but not limited to those of the enzyme genes of the invention, the homologous enzyme gene of the expression host, or any other termination sequence known in the art. Preferred terminators for filamentous fungal host cells are obtained from the genes encoding A. oryzae TAKA amylase, A. niger glucoarnylase, A. nidulans anthranilate synthase, A. niger alpha-glucosidase, and Fusarium oxysporum trypsin-like protease. Preferred terminators for yeast host cells are obtained from the genes encoding Saccharomyces cerevisiae enolase, S. cerevisiae cytochrome C (CYC1), or S. cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, 1995, Molecular Cellular Biology 15:5983-5990.

[0089] For long-term, high-yield production of recombinant proteins, stable expression is preferred. For example, cell lines which stably express the enzyme gene protein can be engineered. Host cells can be transformed with nucleic acid controlled by appropriate expression control elements and a selectable marker. Following the introduction of the foreign nucleic acid, engineered cells can be allowed to grow for 1-2 days in an enriched medium, and then are switched to a selective medium. The selectable marker in the recombinant plasmid confers resistance to the selection after the plasmid integrates into the chromosome via a double cross-over event. Such cells form foci when cultured under selection, which in turn can be cloned and expanded into cell lines. In general, transformants with multiple integrated copies of the expression construct can be obtained by selection and/or amplification, and are preferred since a higher copy number usually results in higher protein production. Alternatively, if an autologously replicating vector is used, the vector can be maintained extrachromosomally in the cells.

[0090] As the vectors of the present invention may be integrated into the host cell genome when introduced into a host cell, the vector may rely on the nucleotide sequence encoding the polypeptide or any other element of the vector for stable integration of the vector into the genome by homologous or nonhomologous recombination. Alternatively, the vector may contain additional nucleic acid sequences for directing integration by homologous recombination into the genome of the host cell. The additional nucleic acid sequences enable the vector to be integrated into the host cell genome at a precise location in a chromosome. To increase the likelihood of integration at a precise location, the integrational elements should preferably contain a sufficient number of nucleic acids, such as 100 to 1,500 base pairs, preferably 400 to 1,500 base pairs, and most preferably 800 to 1,500 base pairs, which are highly homologous with the corresponding target sequence to enhance the probability of homologous recombination. The integrational elements may be any sequence that is homologous with the target sequence in the genome of the host cell. Furthermore, the integrational elements may be nucleic acids comprising non-encoding or encoding nucleotide sequences. On the other hand, the vector may be integrated into the genome of the host cell by non-homologous recombination. These nucleic acids may comprise sequence that is homologous with a target sequence in the genome of the host cell, and, furthermore, may be non-encoding or encoding sequences.

[0091] In one particular embodiment, the enzyme gene of the invention replaces the homolgous enzyme gene of the expression host. The replacement can be effected by any techniques, including homologous recombination. The enzyme gene of the invention can be expressed by regulatory elements associated with the homologous gene in the chromosome or by heterologous regulatory elements. One advantage of this approach is the likelihood that expression of the enzyme gene will be similar to that of the homologous gene. Another advantage of such an expression host is simplification of purification of the desired enzyme, since the native homolgous enzyme is not produced.

[0092] A selection or selectable marker may or may not be part of the nucleic acid vector comprising the enzyme gene sequence. Typically, a selectable marker is a gene the product of which provides for drug or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like. The selection marker will have its own regulatory regions to allow for independent expression of the marker. A large number of transcriptional regulatory regions, preferably regions from genes that are under constituitive expression, are known and may be used in conjunction with the marker gene. Since the recombinant enzyme gene sequences of the invention are preferably introduced into a host that can be used for industrial production, selection markers to monitor the transformation are preferably dominant selection markers, i.e., no mutations have to be introduced into the host strain to be able to use these selection markers. Examples of dominant selectable markers that confer resistance to antibiotics include but are not limited to the ble gene that confers resistance to phleomycin (Austin et al., Gene 1990, 93:157-162), the hph gene that confers resistance to hygromycin B (Tang et al., 1992, Mol. Microbiol., 6:1663-1671), the benA gene that confers resistance to Benomyl (Seip et al., 1990, Appl. Environ. Microbiol. 56:3686-3692); the oligomycin-resistant ATP synthase subunit gene (oliC, Ward et al., 1988, Curr. Genet. 14:37); the bar gene (phosphinothricin acetyltransferase) and the gene that confers glufosinate resistance. Examples of bacterial selectable markers are the dal genes from Bacillus subtilis or Bacillus licheniformis, or markers which confer antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracycline resistance. Where antibiotic resistance is employed, the concentration of the antibiotic for selection will vary depending upon the antibiotic, generally ranging from about 30 to 300 g/ml of the antibiotic.

[0093] The other type of selection markers are nutritional markers that are used for complementation in specific types of mutant cells. For example, transformation of A. nidulans has been demonstrated by using plasmids containing the Neurospora crassa pyr-4 gene (Ballance, D. J. et al., Biochem. Biophys. Res. Commun., 112 (1983):284-289), the A. nidulans amdS gene (Tilburn, J. G. et al., Gene 26 (1983):205-221), the A. nidulans trpC gene (anthranilate synthase; Yelton, M. M. et al., Proc. Natl. Acad. Sci. U.S.A., 81 (1984):1470-1474) and the A. nidulans argb gene (John, M. A. and Peberdy J., Microb. Technol. 6 (1984):386-389). Transformation of Aspergillus niger with the amdS gene of A. nidulans was also described (Kelly, J. M. and Hynes, M. J., EMBO Journal 4 (1985), 475479) and amdS was shown to be a selection marker for use in transformation of A. niger that cannot grow strongly on acetamide as a sole nitrogen source. Transformation of A. niger using the argb gene of A. nidulans has also been described (Buxton, F. P. et al., Gene 37 (1985),207-214). Other examples of nutritional markers may include but are not limited to sC (sulfate adenyltransferase), nitrate utilization (niaD, Unkles et al., 1989, Gene 78:157-166); quinic acid utilization (qutE; Streatfield et al., 1992, Mol. Gen. Genet 233:231-240), and pyrG which complements a orotidine-5′-phosphate decarboxylase mutant (Weidner et al., Curr Genet 1998 May;33(5):378-85). Preferred for use in an Aspergillus cell are the amdS and pyrG markers of A. nidulans or A. oryzae and the bar marker of Streptomyces hygroscopicus. Suitable markers for yeast host cells are ADE2, HIS3, LEU2, LYS2, MET3, TRP1, URA3, and NST (nouseothricin resistance).

[0094] The expression host cells or transformants of the invention maybe cultured in any nutrient medium suitable for growth and expression of proteins. Low concentrations of a protease inhibitor may be employed (if the enzyme to be produced is not a protease), such as phenylmethylsulfonyl fluoride, leupeptin, α2-macroglobulins, pepstatin, or the like. Usually, the concentration will be in the range of about 1 μg/ml to 1 mg/ml. However, in some instances, the protease gene(s) of the expression host may be inactivated in order to avoid or reduce degradation of the desired protein. For example, the host cell may be cultivated by shake flask cultivation, small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid state fermentations) in laboratory or industrial fermentors performed under conditions allowing the polypeptide to be expressed and/or isolated. The cultivation takes place in a suitable nutrient medium comprising carbon and nitrogen sources and inorganic salts, using procedures known in the art (see, e.g., references for bacteria and yeast; Bennett, J. W. and LaSure, L., editors, More Gene Manipulations in Fungi, Academic Press, CA, 1991). Suitable media are available from commercial suppliers or may be prepared according to published compositions (e.g., in catalogues of the American Type Culture Collection). For example, for a fungal fermentation, spores and subsequently cells are transferred through a series of batch fermentations in Erlenmeyer flasks to a 10 liter fermentor. After growth in batch culture, the contents of the 10 liter fermentor are used as inoculum for a final 500 liter batch fermentation.

[0095] If the polypeptide is secreted into the nutrient medium, the polypeptide can be recovered directly from the medium. If the polypeptide is not secreted, it is recovered from cell lysates. The polypeptides may be detected using methods known in the art that are specific for the polypeptides. These detection methods may include use of specific antibodies, formation of an enzyme product, or disappearance of an enzyme substrate. An enzyme assay may be used to determine the activity of the polypeptide. Various methods for concentrating, and purifying the product if necessary, may be employed, such as filtration, centrifugation, solvent-solvent extraction, combinations thereof, or the like.

[0096] Protein purification techniques are well known in the art. Chromatographic methods such as ion-exchange chromatography, gel filtration, use of hydroxyapaptite columns, immobilized reactive dyes, chromatofocusing, and use of high-performance liquid chromatography (HPLC), maybe used to purify the protein. Electrophoretic methods such as one-dimensional gel electrophoresis, high-resolution two-dimensional polyacrylamide electrophoresis, isoelectric focusing, and others are also contemplated as purification methods. Also, affinity chromatographic methods, comprising solid phase bound-antibody, ligand presenting columns and other affinity chromatographic matrices are contemplated as purification methods in the present invention. Alternatively, epitope tagging of the protein can be used to allow simple one step purification of the protein.

[0097] A variety of non-fungal host-expression vector systems can also be utilized to express the enzyme gene coding sequences of the invention. Such host-expression systems represent vehicles by which the coding sequences of interest can be produced and subsequently purified, but also represent cells which can, when transformed or transfected with the appropriate nucleotide coding sequences, produce the enzyme gene protein of the invention in situ. These include but are not limited to microorganisms such as bacteria (e.g., E. coli, B. subtilis) transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing enzyme gene protein coding sequences; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing the enzyme gene protein coding sequences; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing enzyme gene protein coding sequences; or mammalian cell systems (e.g. COS, CHO, BHK, 293, 3T3) harboring recombinant expression constructs containing promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g. the adenovirus late promoter; the vaccinia virus 7.5K promoter).

[0098] In bacterial systems, a number of expression vectors can be advantageously selected depending upon the use intended for the enzyme gene protein being expressed. For example, when a large quantity of such a protein is to be produced, for the generation of antibodies or to screen peptide libraries, for example, vectors which direct the expression of high levels of fusion protein products that are readily purified can be desirable. Such vectors include, but are not limited, to the E. coli expression vector pUR278 Luther et al., 1983, EMBO J. 2:1791), in which the enzyme gene protein coding sequence can be ligated individually into the vector in frame with the lacZ coding region so that a fusion protein is produced; pIN vectors (Inouye & Inouye, 1985, Nucleic Acids Res. 13:3101-3109; Van Heeke & Schuster, 1989, J. Biol. Chem. 264:5503-5509); and the like. pGEX vectors can also be used to express foreign polypeptides as fusion proteins with glutathione S-transferase (GST). In general, such fusion proteins are soluble and can easily be purified from lysed cells by adsorption to glutathione-agarose beads followed by elution in the presence of free glutathione. The pGEX vectors are designed to include thrombin or factor Xa protease cleavage sites so that the cloned enzyme gene protein can be released from the GST moiety. For expression in bacteria, useful regulatory elements include but are not limited to the lac system, the trp system, the tet system and other antibiotic-based repression systems (e.g. PIP), the TAC system (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA 80:21-25), the TRC system, the major operator and promoter regions of phage A, and the control regions of fd coat protein. Other examples of useful promoters may include that of the Streptomyces coelicolor agarase gene (dagA), the Bacillus subtilis levansucrase gene (sacB), the Bacillus licheniformis alpha-amylase gene (amyL), the Bacillus stearothennophilus maltogenic amylase gene (amyM), the Bacillus amyloliquefaciens alphα-amylase gene (amyQ), the Bacillus licheniformis penicillinase gene (penP), and the Bacillus subtilis xylA and xylB genes.

[0099] The choice of a bacterial host cell will to a large extent depend upon the enzyme gene and its application. The host cell may be a bacteria that have been used for producing industrial enzymes. Useful host cells are bacterial cells such as gram positive bacteria including, but not limited to, a Bacillus cell, e.g., Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothernophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, and Bacillus thuringiensis; or a Streptomyces cell, e.g., Streptomyces lividans or Streptomyces murinus. In a preferred embodiment, the bacterial host cell is a Bacillus lentus, a Bacillus licheniformis, a Bacillus subtilis, or a Bacillus stearothermophilus cell. The transformation of a bacterial host cell may, for instance, be effected by protoplast transformation (see, e.g., Chang and Cohen, 1979, Molecular General Genetics 168:111-115), by using competent cells (see, e.g., Young and Spizizin, 1961, Journal of Bacteriology 81:823-829, or Dubnar and Davidoff-Abelson, 1971, Journal of Molecular Biology 56:209-221), by electroporation (see, e.g., Shigekawa and Dower, 1988, Biotechniques 6:742-751), orby conjugation (see, e.g., Koehler and Thome, 1987, Journal of Bacteriology 169:5771-5278).

[0100] 5.3. Aspergillus fumigatus Gene Products

[0101] The enzyme gene products encompassed in the present invention include those gene products (e.g., RNA or proteins) that are encoded by the enzyme gene sequences as described above, such as, the enzyme gene sequences set forth in SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, and 71. The enzyme gene products of the invention also encompasses those RNA or proteins that are encoded by the the genomic sequences of the enzyme genes as set forth in SEQ ID NO 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70. The enzymes of the invention comprises an amino acid sequence selected from the group consisting of SEQ ID NO. 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72.

[0102] The enzymes of the invention display at least one of the chemical characteristics or activity of an enzyme selected from the group consisting of tannase, cellulase, glucose oxidase, glucoamylase, α-amylase, phytase, β-galactosidase, sucrase, lipase, laccase, xylanase and polygalacturonase. As used herein, the term “chemical characteristic” of an enzyme of the invention refers to the substrate or chemical functionality upon which the enzyme acts and/or the catalytic reaction performed by the enzyme; e.g., the catalytic reaction may be hydrolysis (hydrolases) and the chemical functionality may be the type of bond upon which the enzyme acts (esterases cleave ester bonds) or may be the particular type of structure upon which the enzyme acts (a glycosidase which acts on glycosidic bonds).

[0103] As used herein, a “physical characteristic” with respect to an enzyme means a property (other than a chemical characteristic), such as optimum pH for catalytic reaction; temperature stability; optimum temperature for catalytic reaction; organic solvent tolerance; metal ion selectivity, detergent tolerance, etc. The enzymes of the invention can catalyzes their respective enzymatic reaction at a range of temperatures from ambient temperature to elevated temperature, for example, room temperature, i.e., 20° to 25° C., body temperature, i.e, about 37° C., and higher temperatures such as 45° C., 50° C., 55° C., 60° C. and up to 70° C. Since A. fumigatus is a thermophilic fungus, the enzymes of this organism are expected to be stable at 70° C., and even at higher temperature up to 100° C. See Latge, 1999, Clin. Microbiol. Rev. 12:210-350 and Pasarnontes et al., 1997 Applied Environ. Microbiol. 63:1696-1700. The spores of A. fumigatus are also known to survive at extreme low temperature. Accordingly, the enzymes of the invention are also expected to display enzymatic activity and/or stability at low temperatures, e.g., below 10° C., 4° C., −20° C., and −80° C. The enzymes of the invention also display increased half-life in storage and increased organic solvent tolerance.

[0104] The enzyme gene products of the invention can be readily produced, e.g., by synthetic techniques or by methods of recombinant DNA technology using techniques that are well known in the art. In one embodiment, the polypeptides and peptides of the invention can be synthesized or prepared by techniques well known in the art. See, for example, Creighton, 1983, Proteins: Structures and Molecular Principles, W. H. Freeman and Co., N.Y.

[0105] In addition, the methods and compositions of the invention also encompass proteins and polypeptides that represent functionally equivalent gene products. Such functionally equivalent gene products include, but are not limited to, natural variants of the polypeptides having an amino acid sequence set forth in SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72.

[0106] Such equivalent enzyme gene products can contain, e.g. deletions, additions or substitutions of amino acid residues within the amino acid sequences encoded by the enzyme gene sequences described above, but which result in a silent change, thus producing a functionally equivalent product. Amino acid substitutions can be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the residues involved. For example, nonpolar (i.e., hydrophobic) amino acid residues can include alanine (Ala or A), leucine (Leu or L), isoleucine (Ile or I), valine (Val or V), proline (Pro or P), phenylalanine (Phe or F), tryptophan (Trp or W) and methionine (Met or M); polar neutral amino acid residues can include glycine (Gly or G), serine (Ser or S), threonine (Thr or T), cysteine (Cys or C), tyrosine (Tyr or Y), asparagine (Asn or N) and glutamine (Gln or Q); positively charged (i.e., basic) amino acid residues can include arginine (Arg or R), lysine (Lys or K) and histidine (His or H); and negatively charged (i.e., acidic) amino acid residues can include aspartic acid (Asp or D) and glutamic acid (Glu or E).

[0107] “Functionally equivalent,” as the term is utilized herein, refers to a polypeptide capable of exhibiting a substantially similar enzymatic activity or at least one chemical characteristics as the Aspergillus fumigatus enzyme gene product encoded by one of the enzyme gene sequences described in Table 1. Alternatively, the term “functionally equivalent” can refer to peptides or polypeptides that are capable of interacting with the substrate of an enzyme gene of the invention in a manner substantially similar to the way in which the enzyme gene product would interact with such a substrate. Preferably, the functionally equivalent enzyme gene products of the invention are about the same size and display similar physical characteristics as the enzyme encoded by one of the enzyme gene sequences described in Table 1.

[0108] It will be apparent to those skilled in the art that such substitutions can be made outside the regions critical to the function of the molecule and still result in an active polypeptide. Amino acid residues essential to the activity of the polypeptide encoded by the isolated nucleic acid sequence of the invention, and therefore preferably not subject to substitution, may be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (see, e.g., Cunningham and Wells, 1989, Science 244:1081-1085). In the latter technique mutations are introduced at every residue in the molecule, and the resultant mutant molecules are tested for the enzyme activity to identify amino acid residues that are critical to the activity of the molecule. Sites of substrate-enzyme interaction can also be determined by analysis of crystal structure as determined by such techniques as nuclear magnetic resonance analysis, crystallography or photoaffinity labelling (see, e.g., de Vos et al., 1992, Science 255, 306-312; Smith et al., 1992, Journal of Molecular Biology 224:899-904; Wlodaver et al., 1992, FEBS Letters 309, 59-64).

[0109] Peptides and polypeptides corresponding to one or more domains of the enzyme gene products (e.g., signal sequences, active sites, or substrate-binding domains), truncated or deleted enzymes (e.g., polypeptides in which one or more domains of a enzyme are deleted) and fusion enzymes (e.g., proteins in which a full length or truncated or deleted enzyme, or a peptide or polypeptide corresponding to one or more domains of an enzyme is fused to an unrelated protein) are also within the scope of the present invention. Such peptides and polypeptides (also referred to as chimeric protein or polypeptides) can be readily designed by those skilled in the art on the basis of the enzyme gene nucleotide and amino acid sequences listed in Table 1. Exemplary fusion proteins can include, but are not limited to, epitope tag-fusion proteins which facilitates isolation of the enzyme gene product by affinity chromatography using reagents that binds the epitope. Other exemplary fusion proteins include fusions to any amino acid sequence that allows, e.g., the fusion protein to be immobilized onto a solid phase, thereby allowing the enzyme to be retained and re-used after a reaction; the fusion protein to be anchored to a cell membrane, thereby allowing the enzyme to be exhibited on a cell surface; or to a luminescent protein which can provide a marker function. Accordingly, the invention provides a fusion protein comprising a fragment of a first polypeptide fused to a second polypeptide, said fragment of the first polypeptide consisting of at least 6 consecutive residues of an amino acid sequence selected from one of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72.

[0110] Other modifications of the enzyme gene product coding sequences described above can be made to generate polypeptides that are better suited, e.g., for expression, for scale up, etc. in a chosen host cell. For example, cysteine residues can be deleted or substituted with another amino acid in order to eliminate disulfide bridges.

[0111] The enzyme gene products of the invention preferably comprise at least as many contiguous amino acid residues as are necessary to represent an epitope fragment (that is, for the gene products to be recognized by an antibody directed to the enzyme gene product). For example, such protein fragments or peptides can comprise at least about 8 contiguous amino acid residues from a enzyme gene product. In alternative embodiments, the protein fragments and peptides of the invention can comprise about 6, 8, 10, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 150, 200, 250, 300, 350, 400, 450 or more contiguous amino acid residues of a enzyme gene product.

[0112] The enzyme gene products used and encompassed in the methods and compositions of the present invention also encompass amino acid sequences encoded by one or more of the above-described enzyme gene sequences of the invention wherein domains often encoded by one or more exons of those sequences, or fragments thereof, have been deleted. The enzyme gene products of the invention can still further comprise post translational modifications, including, but not limited to, glycosylations, acetylations and myristylations.

[0113] Depending on the industrial application, the enzyme gene protein can be labeled, either directly or indirectly, to facilitate its detection. Any of a variety of suitable labeling systems can be used including but not limited to radioisotopes such as ¹²⁵I; enzyme labeling systems that generate a detectable colorimetric signal or light when exposed to substrate; and fluorescent labels. Indirect labeling involves the use of a protein, such as a labeled antibody, which specifically binds to either a enzyme gene product. Such antibodies include but are not limited to polyclonal antibodies, monoclonal antibodies (mAbs), human, humanized or chimeric antibodies, single chain antibodies, Fab fragments, F(ab′)₂ fragments, fragments produced by a Fab expression library, anti-idiotypic (anti-Id) antibodies, and epitope-binding fragments of any of the above.

[0114] Enzymes of the invention can be used on an industrial scale as catalysts for processing various crude or raw materials. The invention encompasses enzymatic compositions comprising a catalytically effective amount of an enzyme of the invention isolated, purified or enriched to various degrees, e.g., the enzyme can constitute about 0.1%, 0.25%, 0.5%, 0.75%, 1%, 2%, 5%, 10%, 20%, 40%, 50%, 75%, 80%, 90%, 95%, 99% of the total protein in the composition. The enzymatic compositions are in a form suitable for use in the intended industrial processes, and may contain additional enzymes, stabilizing agents, preservatives, protease inhibitors, detergents, antifoaming agents, etc. Often these processes are cost-effective only when the enzymes can be re-used many times. For reuse of the enzymes, the enzymes need to be separated from the bulk of the process. This can be achieved when the enzymes are attached to a carrier or solid phase which can be isolated, for example by draining, filtration or centrifugation. This can also be achieved if the substrate is flowed across the surface of the solid phase where contacts with the enzymes are made. Accordingly, the present invention encompasses enzymes of the invention which exist not only in free-flowing soluble form, but also in immobilized or solid forms.

[0115] In one embodiment, the enzymes of the invention can be stabilized by their association with cell membranes, or whole microbial cells, viable or non-viable. Cells can be further stabilized by entrapment in various kinds of gel or attached to the surface of solid particles. Alternatively, the cells are homogenized and cross-linked with glutaraldehyde to form an insoluble yet permeable matrix. Accordingly, the invention encompasses immobilized cell compositions or cell lysate compositions comprising an enzyme of the invention.

[0116] In another embodiment, the enzymes of the invention are immobilized in the form of proteins purified to varying degrees as described above. Any known method for immobilization of enzyme based on chemical and physical binding of the enzyme to a soild phase, e.g, polysaccharides, glass, synthetic polymers, magnetic particles, which are usually modified with functional groups, such as amine, carboxy, epoxy, phenyl or alkane to enable covalent coupling to amino acid side chains on the enzyme surface, can be used. The solid phase can be porous, with pore diameters in the range of 30 to 300 nm. Ionic and non-ionic adsorption to porous support can be a simple and effective method of immobilization. The enzymes can also be entrapped or encapsulated in polymeric gels, membranes, or micelles in surfactant-stabilized aqueous droplets. The choice of a suitable immobilization method for a given enzyme depends enzyme characteristics, process demands, properties of support, and safety issues, and can be determined by one of skill in the art. Methods for immobilization of enzymes can be found, for example, in Methods of Enzymology, vol. 44, 135, 136, and 137, Academic Press, New York. Accordingly, the invention encompasses an enzymatic composition which comprises one or more solid phase(s), wherein a catalytically active enzyme of the invention is present on the solid phase(s).

[0117] The invention further encompasses enzymes of the invention in solid form. Enzymes in solid form or enzyme granulate can be used, for example, in solid detergent and in animal feed. Methods of making solid forms of enzymes are well known in the art, such as but not limited to prilling (spray-cooling in a waxy material), extrusion, agglomeration, or granulation (dilution with an inert material and binders). Solid enzymatic compositions comprising a solid form of an enzyme of the invention, in the form of mixed powder, tablets, and the like, is contemplated.

[0118] 5.4. Isolation and Use of Antibodies Recognizing Products Encoded by Aspergillus fumigatus Enzyme Genes

[0119] Described herein are methods for the production of antibodies capable of specifically recognizing epitopes of one or more of the enzyme gene products described above. Such antibodies can include, but are not limited to, polyclonal antibodies, monoclonal antibodies (mAbs), human, humanized or chimeric antibodies, single chain antibodies, Fab fragments, F(ab′)₂ fragments, fragments produced by a Fab expression library, anti-idiotypic (anti-Id) antibodies, and epitope-binding fragments of any of the above.

[0120] For the production of antibodies to an enzyme gene or gene product, various host animals can be immunized by injection with a enzyme gene protein, or a portion thereof. Such host animals can include but are not limited to rabbits, mice, and rats, to name but a few. Various adjuvants can be used to increase the immunological response, depending on the host species, including but not limited to Freund's (complete and incomplete), mineral gels such as aluminum hydroxide, surface active substances such as lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, keyhole limpet hemocyanin, dinitrophenol, and potentially useful human adjuvants such as BCG (bacille Calmette-Guerin) and Corynebacterium parvum. Accordingly, the invention provides a method of eliciting an immune response in an animal, comprising introducing into the animal an immunogenic composition comprising an isolated polypeptide, the amino acid sequence of which comprises at least 6 consecutive residues of one of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, as well as the gene product encoded by genomic sequences of SEQ ID NO: 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70, as expressed by Aspergillus fumigatus.

[0121] Polyclonal antibodies are heterogeneous populations of antibody molecules derived from the sera of animals immunized with an antigen, such as enzyme gene product, or an antigenic functional derivative thereof. For the production of polyclonal antibodies, host animals such as those described above, can be immunized by injection with enzyme gene product supplemented with adjuvants as also described above. The antibody titer in the immunized animal can be monitored over time by standard techniques, such as with an enzyme linked immunosorbent assay (ELISA) using immobilized polypeptide. If desired, the antibody molecules can be isolated from the animal (e.g., from the blood) and further purified by well-known techniques, such as protein A chromatography to obtain the IgG fraction.

[0122] Monoclonal antibodies, which are homogeneous populations of antibodies to a particular antigen, can be obtained by any technique which provides for the production of antibody molecules by continuous cell lines in culture. These include, but are not limited to the hybridoma technique of Kohler and Milstein, (1975, Nature 256:495-497; and U.S. Pat. No. 4,376,110), the human B-cell hybridoma technique (Kosbor et al., 1983, Immunology Today 4:72; Cole et al., 1983, Proc. Natl. Acad. Sci. USA 80:2026-2030), and the EBV-hybridoma technique (Cole et al., 1985, Monoclonal Antibodies And Cancer Therapy, Alan R. Liss, Inc., pp. 77-96). Such antibodies can be of any immunoglobulin class including IgG, IgM, IgE, IgA, IgD and any subclass thereof. The hybridoma producing the mAb of this invention can be cultivated in vitro or in vivo. Production of high titers of mAbs in vivo makes this the presently preferred method of production.

[0123] Alternative to preparing monoclonal antibody-secreting hybridomas, a monoclonal antibody directed against a polypeptide of the invention can be identified and isolated by screening a recombinant combinatorial immunoglobulin library (e.g. an antibody phage display library) with the polypeptide of interest. Kits for generating and screening phage display libraries are commercially available (e.g., the Pharmacia Recombinant Phage Antibody System, Catalog No. 27-9400-01; and the Stratagene SurfZAP™ Phage Display Kit, Catalog No. 240612). Additionally, examples of methods and reagents particularly amenable for use in generating and screening antibody display library can be found in, for example, U.S. Pat. No. 5,223,409; PCT Publication No. WO 92/18619; PCT Publication No. WO 91/17271; PCT Publication No. WO 92/20791; PCT Publication No. WO 92/15679; PCT Publication No. WO 93/01288; PCT Publication No. WO 92/01047; PCT Publication No. WO 92/09690; PCT Publication No. WO 90/02809; Fuchs et al. (1991) Bio/Technology 9:1370-1372; Hay et al. (1992) Hum. Antibod. Hybridomas 3:81-85; Huse et al. (1989) Science 246:1275-1281; Griffiths et al. (1993) EMBO J. 12:725-734.

[0124] Additionally, recombinant antibodies, such as chimeric and humanized monoclonal antibodies, comprising both human and non-human portions, which can be made using standard recombinant DNA techniques, are within the scope of the invention. A chimeric antibody is a molecule in which different portions are derived from different animal species, such as those having a variable region derived from a murine mAb and a human immunoglobulin constant region. (See, e.g., Cabilly et al., U.S. Pat. No. 4,816,567; and Boss et al., U.S. Pat. No. 4,816,397, which are incorporated herein by reference in their entirety.) Humanized antibodies are antibody molecules from non-human species having one or more complementarily determining regions (CDRs) from the non-human species and a framework region from a human immunoglobulin molecule. (See, e.g., Queen, U.S. Pat. No. 5,585,089.) Such chimeric and humanized monoclonal antibodies can be produced by recombinant DNA techniques known in the art, for example using methods described in PCT Publication No. WO 87/02671; European Patent Application 184,187; European Patent Application 171,496; European Patent Application 173,494; PCT Publication No. WO 86/01533; U.S. Pat. No. 4,816,567; European Patent Application 125,023; Better et al. (1988) Science 240:1041-1043; Liu et al (1987) Proc. Natl. Acad. Sci. USA 84:3439-3443; Liu et al. (1987) J. Immunol. 139:3521-3526; Sun et al. (1987) Proc. Natl. Acad. Sci. USA 84:214-218; Nishimura et al. (1987) Canc. Res. 47:999-1005; Wood et al. (1985) Nature 314:446449; and Shaw et al. (1988) J. Natl. Cancer Inst. 80:1553-1559); Morrison (1985) Science 229:1202-1207; Oi et al. (1986) Bio/Techniques 4:214; U.S. Pat. No. 5,225,539; Jones et al. (1986) Nature 321:552-525; Verhoeyan et al. (1988) Science 239:1534; and Beidler et al. (1988) J. Immunol. 141:4053-4060.

[0125] Completely human antibodies are particularly desirable for therapeutic treatment of human patients. Such antibodies can be produced using transgenic mice which are incapable of expressing endogenous immunoglobulin heavy and light chains genes, but which can express human heavy and light chain genes. The transgenic mice are immunized in the normal fashion with a selected antigen, e.g., all or a portion of a polypeptide of the invention. Monoclonal antibodies directed against the antigen can be obtained using conventional hybridoma technology. The human immunoglobulin transgenes harbored by the transgenic mice rearrange during B cell differentiation, and subsequently undergo class switching and somatic mutation. Thus, using such a technique, it is possible to produce therapeutically useful IgG, IgA and IgE antibodies. For an overview of this technology for producing human antibodies, see Lonberg and Huszar (1995, Int. Rev. Immunol. 13:65-93). For a detailed discussion of this technology for producing human antibodies and human monoclonal antibodies and protocols for producing such antibodies, see, e.g., U.S. Pat. Nos. 5,625,126; 5,633,425; 5,569,825; 5,661,016; and 5,545,806.

[0126] Completely human antibodies which recognize a selected epitope can be generated using a technique referred to as “guided selection.” In this approach a selected non-human monoclonal antibody, e.g., a mouse antibody, is used to guide the selection of a completely human antibody recognizing the same epitope. (Jespers et al. (1994) Bio/technology 12:899-903).

[0127] Antibody fragments which recognize specific epitopes can be generated by known techniques. For example, such fragments include but are not limited to: the F(ab′)₂ fragments which can be produced by pepsin digestion of the antibody molecule and the Fab fragments which can be generated by reducing the disulfide bridges of the F(ab′)₂ fragments. Alternatively, Fab expression libraries can be constructed (Huse et al., 1989, Science 246:1275-1281) to allow rapid and easy identification of monoclonal Fab fragments with the desired specificity.

[0128] Antibodies of the present invention may also be described or specified in terms of their binding affinity to a enzyme gene product. Preferred binding affinities include those with a dissociation constant or Kd less than 5×10⁻⁶ M, 10⁻⁶M, 5×10⁻⁷ M, 10⁻⁷M, 5×10⁻⁸ M, 10⁻⁸ M, 5×10⁻⁹ M, 10⁻⁹ M, 5×10⁻¹⁰ M, 10⁻¹⁰ M, 5×10⁻¹¹ M, 10⁻¹¹ M, 5×10⁻¹² M, 10⁻¹² M, 5×10⁻¹³ M, 10⁻¹³ M, 5×10⁻¹⁴ M, 10⁻¹⁴ M, 5×10⁻¹⁵ M, or 10⁻¹⁵ M.

[0129] Antibodies directed against an enzyme gene product or fragment thereof can be used to detect the enzyme gene product in order to evaluate the abundance and pattern of expression of the polypeptide under various environmental conditions, in different morphological forms (mycelium, spores) and stages of an organism's life cycle. Antibodies directed against an enzyme gene product or fragment thereof can be used diagnostically to monitor levels of an enzyme gene product in the tissue of an infected host as part of a clinical testing procedure, e.g., to, for example, determine the efficacy of a given treatment regimen. Detection can be facilitated by coupling the antibody to a detectable substance. Examples of detectable substances include various enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials, and radioactive materials. Examples of suitable enzymes include horseradish peroxidase, alkaline phosphatase, beta-galactosidase, or acetylcholinesterase; examples of suitable prosthetic group complexes include streptavidin/biotin and avidin/biotin; examples of suitable fluorescent materials include umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycoerytrin; an example of a luminescent material includes luminol; examples of bioluminescent materials include luciferase, luciferin, and aequorin, and examples of suitable radioactive material include ¹²⁵I, ¹³¹I, ³⁵S or ³H.

[0130] Further, antibodies directed against an enzyme gene product or fragment thereof can be used therapeutically to treat an infectious disease by preventing infection, and/or inhibiting growth of the pathogen. Antibodies can also be used to modify the enzyme activity of an enzyme gene product.

[0131] 5.5. Uses of the Enzymes

[0132] 5.5.1. Tannases

[0133] The present invention encompasses polypeptides having tannase activity. The amino acid sequence of a first polypeptide of the invention having tannase activity is set forth in SEQ ID NO. 3. The polypeptide of SEQ ID NO: 3, herein referred to as tannase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 2 which is derived from the enzyme gene sequence of SEQ ID NO. 1.

[0134] The amino acid sequence of a second polypeptide of the invention having tannase activity is set forth in SEQ ID NO. 6. The polypeptide of SEQ ID NO: 6, herein referred to as tannase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 4 which is derived from the enzyme gene sequence of SEQ ID NO. 5.

[0135] As used herein the terms “tannase 1” and “tannase 2” encompass respectively, not only the polypeptides of SEQ ID NO: 3 and 6, but also all the enzyme gene products related to SEQ ID NO: 1, 2, 4, and 5 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display tannase activity. In preferred embodiments, homologs of tannase 1 having greater than 48% amino acid sequence identity with tannase 1, and homologs of tannase 2 having greater than 79% amino acid sequence identity with tannase 2, are provided.

[0136] Polypeptides having tannase activity have been used in the tea product-making industry. Green tea leaf (as picked) contains colourless polyphenols known as catechins. The four major catechins in green tea leaf are epicatechin and epigallocatechin and the gallated forms of these catechins (bearing a gallic acid (GA) residue), epicatechin-3-gallate and epigallocatechin-3-gallate. The general reaction catalysed by tannase (tannin acylhydrolase, EC 3.1.1.20) is the cleavage of gallate ester linkages, both on gallated catechins and also from other gallated compounds within the leaf. Tannase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, tannase activity can be determined by a spectrophotometric assay based on protocatechuic acid p-nitrophenyl ester (Iacazio et al., 2000, J. Microbiol. Methods, 42:209-14), or gallate derivative comprising rhodanine (Sharma et al., 2000, Anal. Biochem. 279:85-89).

[0137] Epigallocatechin-3-gallate (EGCG) and epicatechin-3-gallate (ECG) are the most abundant catechins in fresh tea leaves and their gallate ester linkages are cleaved by tannase treatment to yield epicatechin, epigallocatechin and gallic acid. Accordingly, A. fumigatus tannase 1 and/or tarmase 2 can be used to increase the levels of epicatechin, epigallocatechin and gallic acid in a tea extract. Generally, a method for modulating the amount of compounds that comprise a gallate ester linkage in a composition comprising contacting the composition with an enzymatic composition which comprises tannase 1 and/or tannase 2, is provided.

[0138] During oxidative fermentation of green leaf to produce black tea (either solid state fermentation to produce black leaf or slurry fermentation to produce black tea extracts) the catechins undergo oxidative biotransformations, through their quinones, into dimeric compounds known as theaflavins and higher molecular weight compounds known as thearubigins. Theaflavins and thearubigins are responsible for the orange and brown colours of black tea infusions and products as well as making significant contributions to the astringency and body of the made tea. The oxidative polymerisations are a combination of biochemical oxidations mediated by polyphenol oxidase and/or peroxidase enzymes. Theaflavin and theaflavins have been recognized to affect tea flavor and color. Most theaflavins have antioxidant properties and are therefore of great interest to the food and health industries. Tannase treatment of tea leaf extracts at various stages of tea product manufacturing results in a change in the levels of theaflavins and thearubigins. Accordingly, A. fumigatus tannase 1 and/or tannase 2 can be used to modulate the levels of theaflavins and thearubigins in a tea extract. For example, the tannase 1 and/or tannase 2 of the invention can be used in the processes of tea product manufacturing as described in U.S. Pat. No. 6,113,965.

[0139] Black tea extracts are normally produced by a hot or boiling water extraction process. However, the black tea extracts, and particularly dried black tea extract, when made to beverage concentrates, usually become turbid if the beverage or the extract is allowed to cool to room temperature or lower. This turbidity is caused by material present in the original black tea (tea solids which are extracted by hot water, but which are insoluble in cold water). This precipitate, known as “tea cream”, is separated from the infusion, for example by centrifugation. This clouding or creaming, however, has been a serious problem in the preparation of a stable commercial tea concentrate and in the acceptance by the consumer of soluble instant tea powders, particularly of instant ice tea products. Tannase has been used to remove this tea cream or to solubilize the cold water-insoluble constituents of a hot water extract of tea. Accordingly, A. fumigatus tannase 1 and/or tannase 2 can be used to solubilize the cold water-insoluble constituents of a hot water extract of tea, and generally, to improve the clarity of tea products. For example, the tannase 1 and/or tannase 2 of the invention can be used in the processes such as those described in British Patents GB-B-1,413,351 and GB-B-1,380,135, U.S. Pat. Nos. 4,639,375; 5,258,188; 5,445,836; 5,925,389.

[0140] In various embodiments, the tannase 1 and/or tannase 2 of the invention can be used to increase the yield of tea liquor from tea leaves, to improve the color, flavor, and health benefits of a tea product, particularly an instant tea product. The enzymes can also be used in wine making. The invention further encompasses an enzyme composition comprising tannase 1, tannase 2, or both, in free form or in an immobilized form. The enzyme composition may contain additional enzymes, such as but not limited to polyphenol oxidases, cellulases, hernicellulases, pectinases, or laccases.

[0141] 5.5.2. Cellulase

[0142] The present invention encompasses polypeptides having cellulase activity. The amino acid sequence of a polypeptide of the invention having cellulase activity is set forth in SEQ ID NO. 9. The polypeptide of SEQ ID NO: 9, herein referred to as cellulase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 8 which is derived from the enzyme gene sequence of SEQ ID NO. 7. As used herein the terms “cellulase 1” encompasses respectively, not only the polypeptide of SEQ ID NO: 9, but also all the enzyme gene products related to SEQ ID NO: 7 and 8 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display cellulase activity. In a preferred embodiment, homologs of cellulase 1 having greater than 76% amino acid sequence identity with cellulase 1 are provided.

[0143] The general reaction catalysed by cellulase is that of an endoglucanases (E.C. 3.2.1.4), cellobiohydrolases (also called exoglucanase, E.C. 3.2.1.91), or a β-glucosidases.(also called cellobiase, E.C. 3.2.1.21). Endoglucanases hydrolyze β-glycoside bonds internally and randornly along the cellulose chains whereas cellobiohydrolases remove cellobiose molecules from the reducing and non-reducing ends of the chains. β-Glucosidases hydrolyze the cellobiose to two molecules of glucose, and therefore eliminate the inhibition of cellobiose on cellobiohydrolases and endoglucanases. The presence of all three components in a composition is generally known as a complete cellulase system which can efficiently convert crystalline cellulose to glucose. Accordingly, A. fumigatus cellulase 1 can be used in methods that require hydrolysis of cellulose. Generally, a method for modulating the amount of cellulose in a composition comprising contacting the composition with an enzymatic composition which comprises cellulase 1, is provided. Cellulase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, cellulase activity may be determined by a colorimetric assay based on a ferricyanide-molybdoarsenic acid reagent (Holm, 1978, Anal. Biochem. 84:522-532).

[0144] Polypeptides having cellulase activity have been included in detergent compositions for the purposes of enhancing the cleaning ability of the composition. Accordingly, A. fumigatus cellulase 1 can be used as a component of a detergent composition, and in methods of laundering garments in conjunction with other enzymes and surfactants. For example, the cellulase 1 of the invention can be used in the methods or be incorporated into the compositions such as those described in U.S. Pat. Nos. 5,904,736; 5,883,066; 6,020,293; 6,235,697; Great Britain Application Nos. 2,075,028, 2,095,275 and 2,094,826. Cellulase can be used to remove a greyish cast on washed garments containing on the surface disrupted and disordered fibrils caused by mechanical action. Cellulases have also been used for denim garment finishing, to achieve softness and the fashionable wom look traditionally obtained by stone-washing and acid washing. Accordingly, A. fumigatus cellulase 1 can be used for altering the properties of textile fibers including but not limited to cotton. The properties affected by cellulase treatment include but are limited to wettability, absorbancy, softness to the touch, optical properties relating to the reflection of light by dyes in colored fibers on the surface of garments. For example, the cellulase 1 of the invention can be used and incorporated into the compositions as described in U.S. Pat. Nos. 4,738,682; 5,874,293; 5,908,472; 5,916,798; 5,919,697; 6,066,494,. In various embodiments, the cellulase 1 of the invention can be used as a component of a detergent, as a cleaning agent, as a softening agent, or as a color restoring agent.

[0145] Cellulase has also been used to preserve and enhance the nutritive value of forage for silage and to improve the palatability, digestibility and rate of digestion of treated forage by ruminants. Accordingly, A. fumigatus cellulase 1 can be used in methods for reducing the amounts of cellulose in food products or animal feed. The cellulase can be used as additives for feed, digestants, and waste management agents. For example, the cellulase 1 of the invention can be used and included in compositions as described in U.S. Pat. Nos. 5,948,454; 6,042,853.

[0146] The invention further encompasses an enzyme composition comprising cellulase 1 in free form or in an immobilized form. The enzyme composition may contain additional enzymes, such as but not limited to other types of cellulases, hemicellulases, tannases, lipases, or pectinases. In a preferred embodiment, the enzyme composition comprising cellulase 1 is a complete cellulase system.

[0147] 5.5.3. Glucose Oxidases

[0148] The present invention encompasses polypeptides having glucose oxidase activity. The amino acid sequence of a first polypeptide of the invention having glucose oxidase activity is set forth in SEQ ID NO: 12. The polypeptide of SEQ ID NO: 12, herein referred to as glucose oxidase 1, is a gene product encoded by the ORF sequence of SEQ ID NO: 11 which is derived from the enzyme gene sequence of SEQ ID NO. 10. The amino acid sequence of a second polypeptide of the invention having glucose oxidase activity is set forth in SEQ ID NO. 15. The polypeptide of SEQ ID NO: 15, herein referred to as glucose oxidase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 14 which is derived from the enzyme gene sequence of SEQ ID NO. 13. The amino acid sequence of a third polypeptide of the invention having glucose oxidase activity is set forth in SEQ ID NO. 18. The polypeptide of SEQ ID NO: 6, herein referred to as glucose oxidase 3, is a gene product encoded by the ORF sequence of SEQ ID NO. 17 which is derived from the enzyme gene sequence of SEQ ID NO. 16. As used herein the terms “glucose oxidase 1”, “glucose oxidase 2” and “glucose oxidase 3” encompasses respectively, not only the polypeptides of SEQ ID NO: 12, 15, and 18, but also all the enzyme gene products related to SEQ ID NO: 10, 11, 13, 14, 16, and 17 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display glucose oxidase activity. In preferred embodiments, homologs of glucose oxidase 1 having greater than 34% amino acid sequence identity with glucose oxidase 1, homologs of glucose oxidase 2 having greater than 29% amino acid sequence identity with glucose oxidase 2, and homologs of glucose oxidase 3 having greater than 34% amino acid sequence identity with glucose oxidase 3, are provided.

[0149] Enzymes having glucose oxidase activity catalyze the oxidation of glucose to gluconic acid with the concomitant production of hydrogen peroxide. Accordingly, A. fumigatus glucose oxidase 1, glucose oxidase 2, and/or glucose oxidase 3 can be used in methods for producing gluconic acid and hydrogen peroxide. Moreover, the A. fumigatus glucose oxidases can individually or in combination be used to modulate the levels of oxygen, especially in a defined volume of space or in a modified atmosphere, such as but not limited to the spaces between food products, beverages and the packaging. The enzyme(s) can be used as a component of an antioxidant system, or in methods for removing oxygen so as to minimize detrimental oxidative processes in food. For example, the glucose oxidase 1, glucose oxidase 2, and/or glucose oxidase 3 of the invention can be used in the kind of processes described in U.S. Pat. No. 4,996,062 and 6,093,436.

[0150] Generally, a method for modulating the amount of glucose or oxygen in a composition comprising contacting the composition with an enzymatic composition which comprises glucose oxidase 1, glucose oxidase 2 and/or glucose oxidase 3, is provided. Glucose oxidase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, glucose oxidase activity may be determined by measuring a decrease in glucose using a colorimetric assay as described in Blake and McLean (1989, Anal. Biochem. 177:156-160).

[0151] Glucose monitoring is commonly practiced by diabetic individuals to measure the level of glucose in a small amount of blood using a device. Many of these devices detect glucose in a blood sample electrochemically, by detecting the oxidation of blood glucose using glucose oxidase, provided as part of a disposable, single-use electrode system. Glucose monitoring is also performed routinely in various industrial processes such as starch conversion, and fermentation, where glucose is either used as a starting material or generated as an intermediate, a by-product, or an end-product. Accordingly, A. fumigatus glucose oxidase 1, glucose oxidase 2, and/or glucose oxidase 3 can be used in methods for detecting the presence of or measuring the concentration of glucose in a sample, such as body fluids, and fluid streams in industrial processes. For example, the glucose oxidase 1, glucose oxidase 2, and/or glucose oxidase 3 of the invention can be used in the devices and methods disclosed in European Patent No. 0 127 958, and U.S. Pat. Nos. 5,141,868; 5,286,362; 5,288,636; 5,437,999; and 6,241,862.

[0152]A. fumigatus glucose oxidases can also be as a bleach for dyes that have leached out of fabrics to prevent dye transfer in a laundering process, such as the methods described in WO 91/05839. In various embodiments, the glucose oxidase 1, glucose oxidase 2 and/or glucose oxidase 3 of the invention can be used in detergents, in desugaring eggs, in the removal of oxygen from beverages, moist food products, flavors, and hermetically sealed food packages, and in the detection and estimation of glucose in industrial solutions, and in body fluids such as blood and urine. The invention further encompasses an enzyme composition comprising the glucose oxidase 1, glucose oxidase 2 and/or glucose oxidase 3, in free form or in an immobilized form. The invention further encompasses a mechanical composition comprising the glucose oxidase 1, glucose oxidase 2 and/or glucose oxidase 3, which can be a device, or a form suitable for use in a device (e.g., test strips).

[0153] 5.5.4. Phytase

[0154] The present invention encompasses polypeptides having phytase activity. The amino acid sequence of a polypeptide of the invention having phytase activity is set forth in SEQ ID NO. 24. The polypeptide of SEQ ID NO: 24, herein referred to as phytase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 23 which is derived from the enzyme gene sequence of SEQ ID NO. 22. As used herein the terms “phytase 1” encompasses respectively, not only the polypeptide of SEQ ID NO: 24, but also all the enzyme gene products related to SEQ ID NO: 23 and 22 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display phytase activity. In a preferred embodiment, homologs of phytase 1 not from A. fumigatus having greater than 27% amino acid sequence identity with phytase 1 is provided.

[0155] A phytase is an enzyme which catalyzes the hydrolysis of phytate or myoinositol 1,2,3,4,5,6-hexakis dihydrogen phosphate (or for short myo-inositol hexakisphosphate) to (1) myo-inositol and/or (2) mono-, di-, tri-, tetra- and/or penta-phosphates thereof and (3) inorganic phosphate. There are primarily two types of phytases: 3-phytase (myo-inositol hexaphosphate 3-phosphohydrolase, EC 3.1.3.8) and 6-phytase (myo-inositol hexaphosphate 6-phosphohydrolase, EC 3.1.3.26). The 3-phytase hydrolyses first the ester bond at the 3-position, whereas the 6-phytase hydrolyzes first the ester bond at the 6-position. Accordingly, A. fumigatus phytase 1 can be used in degrading phytates, in methods for producing myo-inositol and/or its mono-, di-, tri-, tetra- and/or penta-phosphates from phytates, in methods of modulating the amount of myo-inositol phosphates, or in methods for removing inorganic phosphorous from various myo-inositol phosphates. Phytase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, phytase activity may be determined by measuring the amount of enzyme which liberates inorganic phosphorous from 1.5 mM sodium phytate at the rate of 1 μmol/min at 37 C. and at pH 5.50.

[0156]A. fumigatus phytase 1 of the present invention may be applied to a variety of processes which require the conversion of phytate to inositol and inorganic phosphate. Phytic acid is the primary source of inositol and the primary storage form of phosphate in plant seeds. Seeds, cereal grains and legumes are important components of food and feed preparations, in particular of animal feed preparations. But also in human food cereals and legumes are becoming increasingly important. The phosphate moieties of phytic acid chelates divalent and trivalent cations such as metal ions, including the nutritionally essential ions of calcium, iron, zinc and magnesium as well as the trace minerals manganese, copper and molybdenum. However, phytic acid and its salts, phytates, are often not metabolized, since they are not absorbable from the gastrointestinal system. As a result, food and feed preparations need to be supplemented with inorganic phosphate and other nutritionally essential ions such as iron and calcium. Still further, since phytic acid is not metabolized, the phytate phosphorus is excreted with the manure, resulting in an undesirable phosphate pollution of the environment. Accordingly, A. fumigatus phytase 1 can be used in methods for increasing the nutritive value of food or feed substances. For example, the phytase 1 of the invention can be used and incorporated into the compositions such as those described in U.S. Pat. Nos. 3,297,548; 5,436,156; 6,063,431; 6,221,644.

[0157] In various embodiments, the phytase 1 of the invention can be used as a component of animal feed additives, especially animal feed additives for monogastric animals, such as pigs and poultry. Phytase activity in feed can be determined by a colorimetric assay as described in Engelen et al. (2001, J. AOAC Int. 84:629-633). A. fumigatus phytase 1 can also be used in other industrial processes using substrates that contain phytate such as the starch industry and in fermentation industries, such as the brewing industry. The invention further encompasses an enzyme composition comprising phytase 1 in free form or in an immobilized form. The enzyme composition may contain additional enzymes, such as but not limited to other phytases, and cellulases. The invention also encompasses animal feed compositions comprising plant seeds and A. fumigatus phytase 1.

[0158] 5.5.5. β-Galactosidases

[0159] The present invention encompasses polypeptides having β-galactosidase activity.

[0160] The amino acid sequence of a first polypeptide of the invention having β-galactosidase activity is set forth in SEQ ID NO. 27. The polypeptide of SEQ ID NO: 27, herein referred to as β-galactosidase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 26 which is derived from the enzyme gene sequence of SEQ ID NO. 25. The amino acid sequence of a second polypeptide of the invention having β-galactosidase activity is set forth in SEQ ID NO. 30. The polypeptide of SEQ ID NO: 27, herein referred to as β-galactosidase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 29 which is derived from the enzyme gene sequence of SEQ ID NO. 28. As used herein the terms “β-galactosidase 1 ” and “β-galactosidase 2” encompasses respectively, not only the polypeptides of SEQ ID NO: 27 and 30, but also all the enzyme gene products related to SEQ ID NO: 25, 26, 28, and 29 as described above in section 5.2, including but not limited to splice variants, polypeptide fragments, fusion proteins, and derivatives, that display β-galactosidase activity. In preferred embodiments, homologs of β-galactosidase 1 having greater than 54% amino acid sequence identity with β-galactosidase 1, and homologs of β-galactosidase 2 having greater than 70% amino acid sequence identity with galactosidase 2, are provided.

[0161] β-galactosidase (also known as lactase) is an enzyme capable of hydrolyzing lactose into galactose and glucose, both of which are sweeter and more digestible by humans. Accordingly, A. fumigats β-galactosidase 1 and/or β-galactosidase 2 can be used in methods for producing galactose and/or glucose from lactose, and methods for modulating the level of lactose, galactose and glucose in a composition. For example, cheese whey contains large amounts of lactose, and can thus be used as a source of galactose or glucose after treatment with the β-galactosidase 1 and/or β-galactosidase 2 of the invention.

[0162] Food-grade lactase enzyme preparations have been commercially available. To reduce symptoms of lactose maldigestion, such preparations have been used to hydrolyze lactose in milk prior to consumption or taken in the form of a pill. See, e.g., Corazza et al., Aliment. Pharmacol. Therap. 6:61-66 (1992); Solomons et al., Am. J. Clin. Nutr. 41:222-227 (1985); Rosado et al., J. Am. College Nutr. 5:281-290 (1986); Paige et al., Am. J. Clin. Nutr. 28:818-822 (1975). Accordingly, the β-galactosidase 1 and/or β-galactosidase 2 can be used to make food products that are lactose-reduced or lactose-free, e.g., lactose-free milk. The invention further encompasses an enzyme composition comprising β-galactosidase 1, β-galactosidase 2, or both, in free form or in an immobilized form.

[0163] 5.5.6. Invertase

[0164] The present invention encompasses polypeptides having invertase (or sucrase) activity. The amino acid sequence of a polypeptide of the invention having invertase activity is set forth in SEQ ID NO. 36. The polypeptide of SEQ ID NO: 36, herein referred to as invertase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 35 which is derived from the enzyme gene sequence of SEQ ID NO. 34. As used herein the terms “invertase 1 ” encompasses respectively, not only the polypeptide of SEQ ID NO: 36, but also all the enzyme gene products related to SEQ ID NO: 35 and 34 as described above in section 5.2, including but not limited to splice variants, polypeptide fragments, fusion proteins, and derivatives, that display invertase activity. In a preferred embodiment, homologs of invertase 1 having greater than 29% amino acid sequence identity with invertase 1 is provided.

[0165] The reaction catalysed by invertase is the conversion of sucrose to the hexose sugars glucose and fructose. Accordingly, A. fumigates invertase 1 can be used in methods for making glucose, methods for making fructose, or methods for modulating the levels of sucrose, glucose and fructose in a composition. For example, cane molasses is a by-product containing sucrose which is produced in the sugar-manufacturing industry. Invertase 1 of the invention can be used in a process that convert the sucrose in the molasses into hexoses so that the molasses can be used as a fermentation starting material for the manufacturing of other valuable chemicals, such as amino acids. See, for example, U.S. Pat. Nos. 4,774,183; and 4,543,330.

[0166] The invention further encompass an enzyme composition comprising invertase 1 in free form or in an immobilized form. Invertase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, dehydrogenase-linked assays or a colorimetric assay as described in Carins (1987, Anal. Biochem. 167:270-278) can be used.

[0167] 5.5.7. Lipase

[0168] The present invention encompasses polypeptides having lipase activity. The amino acid sequence of a polypeptide of the invention having lipase activity is set forth in SEQ ID NO. 39. The polypeptide of SEQ ID NO: 39, herein referred to as lipase 1, is a gene product encoded by the ORF sequence of SEQ ID NO.38 which is derived from the enzyme gene sequence of SEQ ID NO.37. As used herein the terms “lipase 1” encompasses respectively, not only the polypeptide of SEQ ID NO: 39, but also all the enzyme gene products related to SEQ ID NO: 38 and 37 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display lipase activity. In a preferred embodiment, homologs of lipase 1 having greater than 61% amino acid sequence identity with lipase 1 is provided. Lipases are a group of enzymes belonging to the esterases, and are also called glyceroester hydrolases or acylglycerol-acylhydrolases. Lipases are employed for their ability to modify the structure and composition of triglyceride oils and fats by hydrolysis, esterification and transesterification reactions. These are equilibrium reactions which in one direction result into hydrolysis of triglycerides into free fatty acids and glycerol, mono- or diglycerides, and in the other direction result into re-esterification of glycerol, monoglycerides and diglycerides into triglycerides. Accordingly, A. fumigatus lipase 1 can be used in methods for degrading oils or fats, or producing fatty acids and alcohols from fats or oils, or in methods for modulating the amounts of triglycerides, in a composition. Many known lipases are characterized by a broad substrate spectrum of activity combined with frequently very high stereoselectivity. The end-products of such a lipase reaction, such as monoesters, maybe used as chiral precursors for a variety of compounds, such as non-naturally occurring amino acids and chiral polyesters. Accordingly, A. fumigatus lipase 1 can be used in methods for preparing fatty acids, esters, or alcohols of high optical purity. See, for example, U.S. Pat. Nos. 6,201,147; 6,210,956. Lipase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For example, lipase activity may be determined by the assay of McKellar (1986, J. Dairy Res. 53:117-127).

[0169] Moreover, lipases have been included in detergent compositions for improved cleaning performance, e.g. used in the enhancement of removal of triglycerides containing soils and stains from fabrics. Lipases have also been used in desizing of the thread of fabric when the size used comprises oils or fat. Accordingly, A. fumigatus lipase 1 can be used in degrading fat and oils in the laundry or textile industry, or added to detergent compositions. For example, the lipase 1 of the invention can be used and incorporated into the compositions as described in U.S. Pat. Nos. 4,769,173; 5,069,809; 6,071,356; and PCT application WO94/03578.

[0170] The invention further encompasses an enzyme composition comprising lipase 1 in free form or in an immobilized form. The enzyme composition may contain additional enzymes, such as but not limited to other types of hemicellulases, tannases, xylanases, lipases, or pectinases.

[0171] 5.5.8. Amylases and Glucoamylases

[0172] The present invention encompasses polypeptides having amylase activity and glucoamylase activity. The amino acid sequence of a first polypeptide of the invention having α-amylase activity is set forth in SEQ ID NO. 42. The polypeptide of SEQ ID NO: 42, herein referred to as α-amylase 1, is a gene product encoded by the ORF sequence of SEQ ID NO: 41 which is derived from the enzyme gene sequence of SEQ ID NO. 40. The amino acid sequence of a second polypeptide of the invention having amylase activity is set forth in SEQ ID NO. 45. The polypeptide of SEQ ID NO: 45, herein referred to as α-amylase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 44 which is derived from the enzyme gene sequence of SEQ ID NO. 43. The amino acid sequence of a third polypeptide of the invention having amylase activity is set forth in SEQ ID NO. 48. The polypeptide of SEQ ID NO: 48, herein referred to as α-amylase 3, is a gene product encoded by the ORF sequence of SEQ ID NO. 47 which is derived from the enzyme gene sequence of SEQ ID NO. 46. As used herein the terms “α-amylase 1”, “α-amylase 2” and “α-amylase 3” encompasses respectively, not only the polypeptides of SEQ ID NO: 42, 45, and 48, but also all the enzyme gene products related to SEQ ID NO: 40, 41, 43, 44, 46, and 47 as described above in section 5.2, including but not limited to splice variants, polypeptide fragments, fusion proteins, and derivatives, that display amylase activity. In preferred embodiments, homologs of α-amylase 1 having greater than 78% amino acid sequence identity with α-amylase 1, homologs of α-amylase 2 having greater than 70% amino acid sequence identity with α-amylase 2, and homologs of α-amylase 3 having greater than 50% amino acid sequence identity with α-amylase 3, are provided.

[0173] The amino acid sequence of a first polypeptide of the invention having glucoamylase activity is set forth in SEQ ID NO. 21. The polypeptide of SEQ ID NO: 21, herein referred to as glucoamylase 1, is a gene product encoded by the ORF sequence of SEQ ID NO: 20 which is derived from the enzyme gene sequence of SEQ ID NO. 19. The amino acid sequence of a second polypeptide of the invention having amylase activity is set forth in SEQ ID NO. 33. The polypeptide of SEQ ID NO: 33, herein referred to as glucoamylase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 32 which is derived from the enzyme gene sequence of SEQ ID NO. 31. The amino acid sequence of a third polypeptide of the invention having amylase activity is set forth in SEQ ID NO. 54. The polypeptide of SEQ ID NO: 54, herein referred to as glucoamylase 3, is a gene product encoded by the ORF sequence of SEQ ID NO. 53 which is derived from the enzyme gene sequence of SEQ ID NO. 52. As used herein the terms “glucoamylase 1”, “glucoamylase 2” and “glucoamylase 3” encompasses respectively, not only the polypeptides of SEQ ID NO: 21, 33, and 54, but also all the enzyme gene products related to SEQ ID NO: 19, 20, 31, 32, 52, and 53 as described above in section 5.2, including but not limited to splice variants, polypeptide fragments, fusion proteins, and derivatives, that display amylase activity. In preferred embodiments, homologs of glucoamylase 1 having greater than 58% amino acid sequence identity with glucoarnylase 1, homologs of glucoamylase 2 having greater than 51% amino acid sequence identity with glucoamylase 2, and homologs of glucoamylase 3 having greater than 68% amino acid sequence identity with glucoamylase 3, are provided.

[0174] Amylases cleave the α-1,4-glycosidic linkages of starch. Glucoamylases hydrolyse the terminal glucose monomers. Amylases and glucoamylase (also known as amyloglucosidase) are used as processing aid to convert starch-bearing raw materials (e.g., corn, potato, wheat, cassaya, barley) to products useful to the food industry, such as starches, starch derivatives and starch saccharification products of different sweetness. The primary steps of starch conversion are liquefaction, saccharification, and isomerization. The first step after a starch slurry is prepared, is heating and enzyme treatment. Thermostable amylases have been used to cleave the α-1,4-glycosidic linkages of pregelatinized starch to reduce the visocosity of the slurry, and to produce maltodextrins of low dextrose-equivalent values (DE <25). Maltodextrins are used as blandtasting functional ingredients, e.g., fillers, stabilizers, thickeners, paste, glues. Accordingly, the A. fumigatus α-amylase 1, α-amylase 2 and/or α-amylase 3, which are thermostable can be used in methods for gelatinizing starch, starch liquefaction, methods for reducing viscosity of a starch slurry, and methods for producing maltodextrins (DE <25, or DE of 8-12, 10-20 or 15-25). Generally, a method for modulating the amounts of starches or maltodextins in a composition comprising contacting the composition with an enzymatic composition which comprises α-amylase 1, α-amylase 2 and/or α-amylase 3, is provided. The invention encompasses an enzyme composition comprising the α-amylase 1, α-amylase 2 and/or α-amylase 3, in free form or in an immobilized form. In preferred embodiments, the α-amylase 1, α-amylase 2 and/or α-amylase 3 of the invention are present in an enzyme composition further comprising other α-amylases, such as bacterial α-amylases, preferably thermostable α-amylases including those derived from Bacillus subtilis and B. licheniformis. α-amylase activity may be measured via a number of assays, the choice of which is not critical to the present invention. For purposes of illustration, α-amylase activity may be determined the colorimetric assay of Winn-Deen et al. (1988, Clin. Chem. 34:2005-8), or the colorimetric and electron spin resonance spectroscopy (ESR) methods described in Marcazzan (1999, J. Biochem. Biophys. Methods, 38:191-202).

[0175] The next step of starch conversion is saccharification which can result in the near-total conversion of starch to glucose. Fungal glucoamylases obtained from A. niger, A. oryzae, A. awamori, which display an exoamylase activity and a low α-1,6-glycosidic cleavage activity (i.e., debranching activity) have been used to make glucose syrup or maltoe syrup with a high DE value (DE>40). Accordingly, the A. fumigatus glucoamylase 1, glucoamylase 2 and/or glucoamylase 3, can be used in methods for saccharification of starch, methods for saccharification of maltodextrin, methods for producing high dextrose syrup, such as high DE maltose syrup (DE>40, and up to 50-55 or 55-70), and methods for producing glucose syrup. Generally, a method for modulating the amounts of starches or maltodextrins in a composition comprising contacting the composition with an enzymatic composition which comprises glucoamylase 1, glucoamylase 2 and/or glucoamylase 3, is provided. The invention encompasses an enzyme composition comprising the glucoamylase 1, glucoamylase 2 and/or glucoamylase 3, in free form or in an immobilized form. In preferred embodiments, the glucoamylase 1, glucoamylase 2 and/or glucoamylase 3 of the invention are present in an enzyme composition further comprising other glucoamylases, β-amylases, and pullulanases.

[0176] For example, the α-amylases and glucoamylases can be used in starch converison processes such as those described in U.S. Pat. Nos. 4,132,595; 4,933,279; 5,180,699; 5,322,778; 5,445,990; and 5,935,826.

[0177] Fungal α-amylases have also been used along with proteases by the baking industry to affect the functional properties of dough and enhances characteristics that are desirable for the automated production of baked goods. Added α-amylases can increase the levels of fermentable monosaccharides and disaccharides in the dough which enhance the growth of baker's yeast. Accordingly, the A. fumigatus α-amylase 1, α-amylase 2 and/or α-amylase 3, can be used in methods for supplementing the amylolytic activity in flour or dough, methods for reducing the viscosity of dough, methods for increasing bread volume, and methods for improving storage properties of baked goods. The invention further encompasses an enzyme composition comprising the α-amylase 1, α-amylase 2 and/or α-amylase 3 of the invention and proteases. For example, the α-amylases can be used in processes for making baked products as described in U.S. Pat. Nos. 4,654,216; 5,352,473; 5,338,552 and 6,068,864.

[0178] Fungal α-amylases and glucoamylases have also been used in the brewing industry during the various stages of the brewing process, or in specific processes, such as barley brewing. The enzymes can be added during the mashing step to generate fermentable sugars from starch in the wort. The enzymes, α-amylases in particular, are used to produce low-carbohydrate “light” beer while glucoamylases maybe added to produce a sweet beer. Fungal α-amylases may be added to promote hydrolysis of residual starch which may contribute to turbidity in the final product. The enzymes can also be added to produce a highly carbonated brewed beverage by hydrolysing the residual starch for a second fermentation. The A. fumigatus α-amylase 1, α-amylase 2, α-amylase 3, glucoarnylase 1, glucoarnylase 2 and/or glucoamylase 3 can be used in any of these processes along with or in place of the fungal enzymes currently used. For example, the α-amylases and glucoamylases can be used in fermentation processes as described in U.S. Pat. Nos. 3,988,204; 5,021,246; and 5,048,385.

[0179] α-amylases have also been used in laundry detergents. The enzyne(s), preferably thernostable, catalyse the degradation of starch stains, and improve cleaning by hydrolysing the starch that binds other dirt and stains to fabric. Accordingly, the A. fumigatus α-amylase 1, α-amylase 2 and/or α-amylase 3, can be used as an additive in detergent compositions, and in methods for laundering fabric or dishwashing. The invention further encompasses a detergent composition comprising the α-amylase 1, α-amylase 2 and/or α-amylase 3 of the invention, surfactants, and other enzymes such as but not limited to proteases, lipases, and cellulases. For example, the α-amylases can be used in cleaning processes as described in U.S. Pat. Nos. 5,851,973; 5,972,040; 6,140,293; and 6,147,045.

[0180] 5.5.9. Laccase

[0181] The present invention encompasses polypeptides having laccase activity. The amino acid sequence of a polypeptide of the invention having laccase activity is set forth in SEQ ID NO. 51. The polypeptide of SEQ ID NO: 51, herein referred to as laccase 1, is a gene product encoded by the ORF sequence of SEQ ID NO. 50 which is derived from the enzyme gene sequence of SEQ ID NO. 49. As used herein the terms “laccase 1” encompasses respectively, not only the polypeptide of SEQ ID NO: 51, but also all the enzyme gene products related to SEQ ID NO: 50 and 49 as described above in section 5.2, including but not limited to splice variants, polypeptide fragments, fusion proteins, and derivatives, that display laccase activity. In a preferred embodiment, homologs of laccase 1 having greater than 46% amino acid sequence identity with laccase 1 is provided.

[0182] Known laccases (benzenediol:oxygen oxidoreductases; E.C. 1.10.3.2) are multi-copper containing enzymes that catalyze the oxidation of phenolics. Laccase-mediated oxidations produce aryloxy-radical intermediates from a phenolic substrate which result in the formation of dimeric to polymeric reaction products. Known laccases exhibits a wide range of substrate specificity. A major problem with the use of known laccases are their poor storage stability at temperatures above room temperature, especially at 40° C. The laccase of the invention is thermostable and can thus be used in many applications that require temperature above room temperature. Laccase activity can be determined by any methods known in the art, such as syringaldazine oxidation monitored at 530 nm, 10-(2-hydroxyethyl)-phenoxazine (HEPO) oxidation which can be monitored photometrically at 528 nm. (G. Cauquil in Bulletin de la Society Chemique de France, 1960, p. 1049), or oxidation of 2,2′-azinobis-(3-ethybenzthiazoline-6-sulfonic acid) (ABTS). Generally, a method for modulating the amounts of oxidated phenolic compounds in a composition comprising contacting the composition with an enzymatic composition which comprises laccase 1, is provided.

[0183] The A. fumigatus laccase 1 may be used in a number of different industrial processes. These processes include polymerization of lignin, both Kraft and lignosulfates, in solution, in order to produce a lignin with a higher molecular weight. For example, laccase 1 of the invention can be used in processes such as those disclosed in U.S. Pat. No. 4,432,921; EP 0 275 544; and PCT/DK93/00217, 1993. Laccase 1 can also be useful in the copolymerization of lignin with low molecular weight compounds, such as is described by Milstein et al., 1994, Appl. Microbiol. Biotechnol. 40: 760-767.

[0184] The laccase 1 of the present invention can also be used for depolymerization of lignin in Kraft pulp, thereby producing a pulp with lower lignin content. This use of laccase is an improvement over the current use of chlorine for depolymerization of lignin, which leads to the production of chlorinated aromatic compounds, which are an environmentally undesirable by-product of paper mills. Such uses are described in, for example, U.S. Pat. No. 6,023,065; Current Opinion in Biotechnology 3: 261-266, 1992; Journal of Biotechnology 25: 333-339,1992; Hiroi et al., 1976, Svensk Papperstidning 5:162-166, 1976.

[0185] Laccase 1 of the invention can also be used in the oxidation of dyes or dye precursors and other chromophoric compounds that leads to decolorization of the compounds. This can be particularly advantageous in a situation in which a dye transfer between fabrics is undesirable, e.g., in the textile industry and in the detergent industry. Methods for bleaching, dye transfer inhibition and dye oxidation using a laccase can be found in U.S. Pat. No. 5,752,890; WO 96/12845; WO 96/12846; WO 92/01406; WO 92/18683; WO 92/18687; WO 91/05839; EP 0495836; Tsujino et al., 1991, J. Soc. Chem. 42: 273-282; which are incorporated herein by reference. Polypeptides having laccase activity can also be used in detergent compositions for the purposes of enhancing the cleaning ability of the composition. Accordingly, A. fumigatus laccase 1 can be used as a component of a detergent composition, and in methods of laundering garments in conjunction with other enzymes and surfectants. For example, the laccase 1 of the invention can be used as described in WO 95/01426.

[0186] The present laccase 1 can also be used for the polymerization or oxidation of phenolic compounds present in liquids. An example of such utility is the treatment of juices, such as apple juice, so that the laccase will accelerate a precipitation of the phenolic compounds present in the juice, thereby producing a more stable juice. Laccase 1 of the present invention can also useful in soil detoxification (Nannipieri et al., 1991, J. Environ. Qual. 20: 510-517; Dec and Bollag, 1990, Arch. Environ. Contam. Toxicol. 19: 543-550). In various embodiments, the laccase 1 of the invention can be used in lignin modification, paper strengthening, dye transfer inhibition in detergents, phenol polymerization, juice manufacture, phenol resin production, and waste water treatment. The invention further encompasses an enzyme composition comprising laccase 1, or both, in free form or in an immobilized form. The enzyme composition may contain additional enzymes, such as but not limited to polyphenol oxidases, cellulases, hemicellulases, and pectinases.

[0187] 5.5.10. Polygalacturonases

[0188] The present invention encompasses polypeptides having polygalacturonase activity. The amino acid sequence of a first polypeptide of the invention having polygalacturonase activity is set forth in SEQ ID NO. 57. The polypeptide of SEQ ID NO: 57, herein referred to as polygalacturonase 1, is a gene product encoded by the ORF sequence of SEQ ID NO: 56 which is derived from the enzyme gene sequence of SEQ ID NO. 55. The amino acid sequence of a second polypeptide of the invention having polygalacturonase activity is set forth in SEQ ID NO. 60. The polypeptide of SEQ ID NO: 60, herein referred to as polygalacturonase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 59 which is derived from the enzyme gene sequence of SEQ ID NO. 58. The amino acid sequence of a third polypeptide of the invention having polygalacturonase activity is set forth in SEQ ID NO. 63. The polypeptide of SEQ ID NO: 63, herein referred to as polygalacturonase 3, is a gene product encoded by the ORF sequence of SEQ ID NO. 62 which is derived from the enzyme gene sequence of SEQ ID NO. 61. As used herein the terms “polygalacturonase 1”, “polygalacturonase 2” and “polygalacturonase 3” encompasses respectively, not only the polypeptides of SEQ ID NO: 57, 60, and 63, but also all the enzyme gene products related to SEQ ID NO: 55, 56, 58, 59, 61, and 62 as described above in section 5.2, including but not limited to homologs, splice variants, polypeptide fragments, fusion proteins, and functional derivatives, that display polygalacturonase activity. In preferred embodiments, homologs of polygalacturonase 1 having greater than 69% amino acid sequence identity with polygalacturonase 1, homologs of polygalacturonase 2 having greater than 80% amino acid sequence identity with polygalacturonase 2, and homologs of polygalacturonase 3 having greater than 80% amino acid sequence identity with polygalacturonase 3, are provided. Enzymes having polygalacturonase activity hydrolyses the glycosidic linkages in a polygalacturonic acid chain which are commonly found in plant cell walls. They exist mainly as chains of 1,4-linked a-D-galacturonic acid and methoxylated derivatives thereof. Accordingly, A. fumigatus polygalacturonases can be used to reduce the amounts of polygalacturonic acid polymers in a composition, or to produce monogalacturonic acid or galacturonic acid containing oligosaccharides from pectin-containing materials.

[0189] The enzymes of the invention are useful in the food industry, primarily in fruit and vegetable processing such as fruit juice production or wine making. For example, A. fumigatus polygalacturonase 1, polygalacturonase 2, and/or polygalacturonase 3 can be used in methods for degrading pectin polymers in plant-derived materials, e.g. obtained from soy beans, sugar beets, apples or pears, so as to reduce the viscosity and thus improve the processing or storage properties of the materials. The enzymes may also be used in the treatment of mash or pulp from fruits and vegetables in order to improve the properties of the mash for processing or disposal. For example, the consistency and appearance of processed fruit or vegetables can be manipulated with the polygalcturonases of the invention. The polygalacturonases of the invention can alone or together with other enzymes be used to improve the digestibility of pectin-containing animal feed. For example, the polygalacturonase 1, polygalacturonase 2, and/or polygalacturonase 3 of the invention can be used in the type of processes described in U.S. Pat. No. 5,830,737 and 6,159,718.

[0190] The invention further encompasses an enzyme composition comprising the polygalacturonase 1, polygalacturonase 2 and/or polygalacturonase 3, in free form or in an immobilized form. The invention further encompasses an eznyme composition comprising polygalacturonase 1, polygalacturonase 2 and/or polygalacturonase 3, and cellulases, xylanases, proteases, and pectin degrading enzymes, such as but not limited to a pectin methyl esterase, a pectin lyase, pectin acetyl esterase, a rhamnogalacturonase, a galactanase, an arabinanase and/or a rharnnogalacturonan acetyl esterase.

[0191] 5.5.11. Xylanases

[0192] The present invention encompasses polypeptides having xylanase activity. The amino acid sequence of a first polypeptide of the invention having xylanase activity is set forth in SEQ ID NO. 66. The polypeptide of SEQ ID NO: 66, herein referred to as xylanase 1, is a gene product encoded by the ORF sequence of SEQ ID NO: 65 which is derived from the enzyme gene sequence of SEQ ID NO. 64. The amino acid sequence of a second polypeptide of the invention having xylanase activity is set forth in SEQ ID NO. 69. The polypeptide of SEQ ID NO: 69, herein referred to as xylanase 2, is a gene product encoded by the ORF sequence of SEQ ID NO. 68 which is derived from the enzyme gene sequence of SEQ ID NO. 67. The amino acid sequence of a third polypeptide of the invention having xylanase activity is set forth in SEQ ID NO. 72. The polypeptide of SEQ ID NO: 72, herein referred to as xylanase 3, is a gene product encoded by the ORF sequence of SEQ ID NO. 71 which is derived from the enzyme gene sequence of SEQ ID NO. 70. As used herein the terms “xylanase 1”, “xylanase 2” and “xylanase 3” encompasses respectively, not only the polypeptides of SEQ ID NO: 66, 69, and 72, but also all the enzyme gene products related to SEQ ID NO: 64, 65, 67, 68, 70, and 71 as described above in section 5.2, including but not limited to homologs, splice variants., polypeptide fragments, fusion proteins, and functional derivatives, that display xylanase activity. In preferred embodiments, homologs of xylanase 1 having greater than 73% amino acid sequence identity with xylanase 1, homologs of xylanase 2 having greater than 77% amino acid sequence identity with xylanase 2, and homologs of xylanase 3 having greater than 79% amino acid sequence identity with xylanase 3, are provided.

[0193] Xylan, a major component of plant hemicellulose, is a polymer of D-xylose linked by β-1,4-xylosidic bonds. Xylan can be degraded to xylose and xylo-oligomers by xylanases (EC3.2.1.8) that randomly cleave the β,1-4 linkages. When this plant cell wall polysaccharide is hydrolyzed with xylanases, it can be exploited as a rich source of carbon and energy for the production of livestock and microorganisms. Accordingly, A. fumigatus xylanase 1, xylanase 2, and/or xylanase 3 can be used in methods for degrading xylan, or methods for producing xylose and xylo-oligomers which may serve as growth substrates for microorganisms in various fermentation processes.

[0194] The A. fumigatus xylanase 1, xylanase 2, and/or xylanase 3 can also be used as an animal feed additive. The treatment of forages with xylanases along with cellulases increase the rate of acid production, thus ensuring better quality silage and improvement in the subsequent rate of plant cell wall digestion by ruminants. The xylanases can also be used to treat rye, and other cereals with a high arabinoxylan content to improve the digestibility of cereal by poultry and swine.

[0195] Enzymatic disruption of plant cell walls can increase the efficiency of a number of industrial processes. For example, the xylanases of the invention can be used in biopulping to treat cellulose pulps to remove xylan impurities or to produce pulps with different characteristics. Further, xylanases of the invention can be useful in the retting of flax fibers, the clarification of fruit juices, the preparation of dextrans for use as food thickeners and the production of fluids and juices from plant materials. For example, the xylanase 1, xylanase 2, and/or xylanase 3 of the invention can be used in the type of processes described in U.S. Pat. No. WO 91/19782, EP 463 706, WO 92/01793, and WO 92/17573. The invention further encompasses an enzyme composition comprising the xylanase 1, xylanase 2 and/or xylanase 3, in free form or in an immobilized form. The invention further encompasses an enzyme composition comprising the xylanase 1, xylanase 2 and/or xylanase 3, and cellulases, and hemicellulases.

6. EXAMPLES

[0196] Described below are techniques used in the analysis of genomic DNA from Aspergillus fumigatus and the cloning and expression of the enzyme genes of the invention.

[0197] 6.1. Isolation of Genomic DNA from Aspergillus fumigatus

[0198] Genomic DNA was isolated from Aspergillus fumigatus strain CEA17 using a commercially available isolation kit (DNEasy Plant Mini Kit, Qiagen, Inc.) according to the manufacturer's instructions with the following minor modifications. Briefly, mycelia were cultured by collecting spores from a confluent plate using a wet inoculating loop and the scraped spores touched to the surface of culture medium placed in a 24 well culture dish. The spores were swirled in the medium to ensure even growth and the dish was incubated without shaking for about 14 to 16 hours at 37° C. The mycelia grow on the surface at the air-medium interface.

[0199] The mycelia were harvested using a sterile toothpick and placed between sterile paper towels. The mycelia were squeezed to remove excess liquid and the harvested mycelia were allowed to dry for 5-10 minutes. The semi-dry mycelia were placed into Bio101 Homogenizing Matrix tubes using a sterile toothpick. To each tube, 400 μl of lysis buffer (Buffer AP1) was added and the tubes were placed into the Bio101 FastPrep Apparatus (Qbiogene), run at a speed setting of 5 for 30 seconds, and then subjected to centrifugation in a nicrofuge for two minutes at maximum speed at 4° C.

[0200] The supernatant containing the genomic DNA was transferred to a sterile 1.5 ml tube, 4 μl of 100 mg/mL solution of RNase was added to each tube, and the tubes were incubated for 10 minutes at 65° C. Approximately 130 μl of protein precipitation buffer (Buffer AP2) was added, the tubes mixed and incubated for about 5 minutes on ice. The supernatant was applied to the supplied QIAshredder spin column (lilac) sitting in a 2 ml collection tube and subjected to centrifugation in a microfuge for 2 min at maximum speed. The flow-through fraction was transferred to a sterile tube without disturbing the cell-debris pellet, 0.5-volume of DNA precipitation buffer (Buffer AP3) and 1 volume of ethanol (96-100%) were added to the cleared supematant and the tubes mixed by inverting a couple times. The supematant was applied in 650 μl aliquots, including any precipitate that may have formed, to the supplied DNeasy mini-spin column sitting in a 2 ml collection tube (supplied). The column was subjected to centrifugation in a microfuge for 1 minute at >8000 rpm and flow-through and the collection tube were discarded. The DNEasy column was placed in the supplied 2 ml collection tube, 500 μl of wash buffer (Buffer AW) was added and the DNeasy column was subjected to centrifugation in a microfuge at >8000 rpm for about 1 minute. The flow-through was discarded and the genomic DNA was eluted twice by the addition of 100 μl of a preheated (56° C.-65° C.) elution buffer (Buffer AE). The above-described protocol typically results in ˜50-100 ng of genomic DNA/μl (approximately 200 μl elution volume).

[0201] 6.2. Transformation of Aspergillus fumigatus Protoplasts

[0202] 6.2.1. Growth and Harvest of Mycelia

[0203] An aliquot of approximate 10⁹ spores of Aspergillus fumigatus CEA17 was inoculated into 250 ml of non-selective medium supplemented with uridine and uracil, e.g., Aspergillus complete medium (ACM), and the culture was incubated with shaking at 250 rpm for about 14 to 16 hours at 30° C. After incubation, the culture is checked under a microscope to determine whether balls of mycelia have formed. If balls of mycelia are not evident, the culture was shifted to 37° C. and incubated for another 2-3 hours to stimulate mycelia ball formation. Approximately 10 transformation procedures can be performed from 250 ml of primary culture.

[0204] The mycelia were collected by filtration using a vacuum flask adapted with a sterile, cheesecloth-lined funnel. The collected mycelia were washed with 25 ml of a sterile solution of cold 0.6 M MgSO₄ and the washed mycelia were allowed to dry for about one minute. The mycelia were harvested using a sterile spatula to remove the mycelia from the cheesecloth and placed in a tube. The mass of mycelia should optimally occupy no more than 20% of the volume of the tube for optimal protoplast formation.

[0205] 6.2.2. Generation and Collection of Protoplasts

[0206] Approximately a 10 ml volume of collected mycelia was placed in a 50 ml conical tube, and a sterile solution of osmotic medium (1.2 M MgSO₄, 10 mM NaPO₄, pH 5.8) is added to the tube to a final volume of 50 ml. The mycelia were dispersed by vortexing for 0.5 to 1 minute. In a separate 2 ml tube, 250 mg of Driselase enzyme (Interspex Products, San Mateo, Calif.) was added to about 1 ml of osmotic medium and placed on ice for 5 minutes. The tube was subjected to brief centrifugation at 14,000×G for 30 seconds to pellet the enzyme starch carrier. Failure to remove the starch carrier may interfere with obtaining protoplasts. The enzyme supematant was transferred to a sterile tube and 400 mg β-D-glucanase (Interspex Products, San Mateo, Calif.) was added. The enzyme mixture was allowed to dissolve, added to the 50 ml mycelia preparation, and mixed by inverting.

[0207] The contents of the tube were poured into 500 ml Erlenmeyer flask and incubated with shaking between 100-125 rpm for 2.5 hours at 30° C. The progress of protoplast formation was examined microscopically at various time intervals until complete. Protoplast formation is typically complete within two hours. The protoplast suspension was dispensed into several 50 ml conical tubes adding no more than 10 ml volume to each tube. The suspension was gently overlaid with an equal volume of sterile Trapping Buffer (0.6 M Sorbitol in 0.1 M Tris-Cl, pH 7.0) being careful not to mix the two layers. The tubes were subjected to centrifugation at 3,000×G in a swinging bucket rotor for 15 minutes. The fuzzy white layer of that forms at the Osmotic medium/Trapping Buffer interface containing the protoplasts was removed using a transfer pipette and the samples were combined.

[0208] The combined samples were placed into a plastic centrifuge tube capable of withstanding up to 10,000×g and an equal volume of sterile STC buffer (1.2 M sorbitol, 10 mM CaCl₂ in 10 mM Tris-HCl, pH 7) was added. The protoplasts were pelleted by subjecting the protoplast sample to centrifugation at 8,000×g for 8 minutes at 4° C. The supernatant of the sample was removed taking care not to disturb the pellet. The pellet was gently resuspended in 5 ml STC buffer using a transfer pipette and the protoplasts were pelleted by subjecting the protoplast sample to centrifugation at 8,000×g for 8 minutes at 4° C. The above-described STC buffer wash steps were repeated an additional two times, the protoplasts were combined into a single tube, and resuspended into an appropriate volume for transformation (approximately 100 μl protoplast suspension/transformation reaction).

[0209] The present invention is not to be limited in scope by the specific embodiments described herein. Indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description and accompanying figures. Such modifications are intended to fall within the scope of the appended claims.

[0210] Various publications and patents are cited throughout the specification. The disclosures of each of these publications and patents are incorporated by reference in its entirety.

1 72 1 1722 DNA Aspergillus 1 atgcgtccct ctagctgcat ccccttctcc gtgggccttg ccgttgtggc ccatgcagcg 60 tctccgtcaa ccctggagga gctctgcacc gtttcatatc ttcaaactgt gttgccttca 120 tctaagttca ttcagggcat caccattgac tcagactctc tcacaaccag tgtggtgacc 180 aacagcactg tcagcagcgt tgactaccct acggcgacga tcgactactg caatgtcacc 240 ctggcctact cgcacgatgg tatcgacggc gaccgagtcc tactccaaat atggctacca 300 gctcctaccg acttccaaaa ccgatggctg tccaccggag gcggtggtta tgccatcaat 360 tccgggacgc gaatgctccc tgagggtatc atctacggtg cggcgtctgg actcacggac 420 ggtgggtttg ggggcttctc ggtgaatgcc gacagcgcta tgttgctggc caacggtaca 480 ctgaactatg aggcgctgta catgttcggg tacaaggctc accgggaact tagcttgatt 540 ggcaaggcct tcacgcggaa ggtctacggc atggccgaca gtgagaagct ctatgcctac 600 taccatggat gctccgaggg tggccgtgag ggctggagcc aagtgcagcg ctacggtgac 660 gaatgggatg gggccattat cggggctcca gcgtttcgtt ggtcgtttca gcagactcaa 720 catctgttct cgaatatcgt tgagaagact cttgactact accctccgcc ctgcgagctg 780 gagaagattg tgaacgagac tatcgttgca tgcgatccct tggacggcag gactgatggt 840 gtggtcgctc gaaccgatct ctgcctgctg catttcgacc tgaaacatgt cattggcaag 900 aagtactcct gcgcggcttc taccaccgca ccggcacaga gtggcactgt ttcagccaag 960 gcagtcgagg tcgctaaaac catcattaac ggactgcatg acactcaggg ccgtcgagtg 1020 tacttctcct accaacccag tgccgcattc gacgatgctc agacgcagtt caatgccgac 1080 accggcaagt gggagctgtc tatcaaccaa ctcgggggca aacacattgc actgctgatg 1140 aacaaaaaca gcaccaccct ggacagccta aacggcgtta cctacgacac gttgaaagac 1200 tggataattt cgggcatgca ggagtactac agcaccctgc agactacctg gcccgatctc 1260 acacccttcc accaggctgg cggcaaagtg atccactacc atggcgacgc tgatttcagc 1320 atccccactg cttcgtctat ccgctactgg gagtcggtgc ggagtaccat gtacggcaac 1380 ctgtcgtaca aagctggtgc taacgcattg aatgaatggt accgcttata cactgtgcct 1440 ggtgccggcc actgctcgac caacgatgcc atgcccaatg gtccatggcc tcagaccaac 1500 ctcgctacca tggtagaatg ggtcgaaaag ggagtgactc cggtcaccct gaatgcaaca 1560 gtgctccagg gcgagtatga aggcgagacc cagcagctct gcgcgtggcc attgcgtcct 1620 ctctggaaga acaaaggaaa gaccctaaac tgtgtgtatg accaggcgtc catcaacagc 1680 tggcactatg acttggatgc agttcctatg cctgtatatt ag 1722 2 1722 DNA Aspergillus CDS (1)...(1722) 2 atg cgt ccc tct agc tgc atc ccc ttc tcc gtg ggc ctt gcc gtt gtg 48 Met Arg Pro Ser Ser Cys Ile Pro Phe Ser Val Gly Leu Ala Val Val 1 5 10 15 gcc cat gca gcg tct ccg tca acc ctg gag gag ctc tgc acc gtt tca 96 Ala His Ala Ala Ser Pro Ser Thr Leu Glu Glu Leu Cys Thr Val Ser 20 25 30 tat ctt caa act gtg ttg cct tca tct aag ttc att cag ggc atc acc 144 Tyr Leu Gln Thr Val Leu Pro Ser Ser Lys Phe Ile Gln Gly Ile Thr 35 40 45 att gac tca gac tct ctc aca acc agt gtg gtg acc aac agc act gtc 192 Ile Asp Ser Asp Ser Leu Thr Thr Ser Val Val Thr Asn Ser Thr Val 50 55 60 agc agc gtt gac tac cct acg gcg acg atc gac tac tgc aat gtc acc 240 Ser Ser Val Asp Tyr Pro Thr Ala Thr Ile Asp Tyr Cys Asn Val Thr 65 70 75 80 ctg gcc tac tcg cac gat ggt atc gac ggc gac cga gtc cta ctc caa 288 Leu Ala Tyr Ser His Asp Gly Ile Asp Gly Asp Arg Val Leu Leu Gln 85 90 95 ata tgg cta cca gct cct acc gac ttc caa aac cga tgg ctg tcc acc 336 Ile Trp Leu Pro Ala Pro Thr Asp Phe Gln Asn Arg Trp Leu Ser Thr 100 105 110 gga ggc ggt ggt tat gcc atc aat tcc ggg acg cga atg ctc cct gag 384 Gly Gly Gly Gly Tyr Ala Ile Asn Ser Gly Thr Arg Met Leu Pro Glu 115 120 125 ggt atc atc tac ggt gcg gcg tct gga ctc acg gac ggt ggg ttt ggg 432 Gly Ile Ile Tyr Gly Ala Ala Ser Gly Leu Thr Asp Gly Gly Phe Gly 130 135 140 ggc ttc tcg gtg aat gcc gac agc gct atg ttg ctg gcc aac ggt aca 480 Gly Phe Ser Val Asn Ala Asp Ser Ala Met Leu Leu Ala Asn Gly Thr 145 150 155 160 ctg aac tat gag gcg ctg tac atg ttc ggg tac aag gct cac cgg gaa 528 Leu Asn Tyr Glu Ala Leu Tyr Met Phe Gly Tyr Lys Ala His Arg Glu 165 170 175 ctt agc ttg att ggc aag gcc ttc acg cgg aag gtc tac ggc atg gcc 576 Leu Ser Leu Ile Gly Lys Ala Phe Thr Arg Lys Val Tyr Gly Met Ala 180 185 190 gac agt gag aag ctc tat gcc tac tac cat gga tgc tcc gag ggt ggc 624 Asp Ser Glu Lys Leu Tyr Ala Tyr Tyr His Gly Cys Ser Glu Gly Gly 195 200 205 cgt gag ggc tgg agc caa gtg cag cgc tac ggt gac gaa tgg gat ggg 672 Arg Glu Gly Trp Ser Gln Val Gln Arg Tyr Gly Asp Glu Trp Asp Gly 210 215 220 gcc att atc ggg gct cca gcg ttt cgt tgg tcg ttt cag cag act caa 720 Ala Ile Ile Gly Ala Pro Ala Phe Arg Trp Ser Phe Gln Gln Thr Gln 225 230 235 240 cat ctg ttc tcg aat atc gtt gag aag act ctt gac tac tac cct ccg 768 His Leu Phe Ser Asn Ile Val Glu Lys Thr Leu Asp Tyr Tyr Pro Pro 245 250 255 ccc tgc gag ctg gag aag att gtg aac gag act atc gtt gca tgc gat 816 Pro Cys Glu Leu Glu Lys Ile Val Asn Glu Thr Ile Val Ala Cys Asp 260 265 270 ccc ttg gac ggc agg act gat ggt gtg gtc gct cga acc gat ctc tgc 864 Pro Leu Asp Gly Arg Thr Asp Gly Val Val Ala Arg Thr Asp Leu Cys 275 280 285 ctg ctg cat ttc gac ctg aaa cat gtc att ggc aag aag tac tcc tgc 912 Leu Leu His Phe Asp Leu Lys His Val Ile Gly Lys Lys Tyr Ser Cys 290 295 300 gcg gct tct acc acc gca ccg gca cag agt ggc act gtt tca gcc aag 960 Ala Ala Ser Thr Thr Ala Pro Ala Gln Ser Gly Thr Val Ser Ala Lys 305 310 315 320 gca gtc gag gtc gct aaa acc atc att aac gga ctg cat gac act cag 1008 Ala Val Glu Val Ala Lys Thr Ile Ile Asn Gly Leu His Asp Thr Gln 325 330 335 ggc cgt cga gtg tac ttc tcc tac caa ccc agt gcc gca ttc gac gat 1056 Gly Arg Arg Val Tyr Phe Ser Tyr Gln Pro Ser Ala Ala Phe Asp Asp 340 345 350 gct cag acg cag ttc aat gcc gac acc ggc aag tgg gag ctg tct atc 1104 Ala Gln Thr Gln Phe Asn Ala Asp Thr Gly Lys Trp Glu Leu Ser Ile 355 360 365 aac caa ctc ggg ggc aaa cac att gca ctg ctg atg aac aaa aac agc 1152 Asn Gln Leu Gly Gly Lys His Ile Ala Leu Leu Met Asn Lys Asn Ser 370 375 380 acc acc ctg gac agc cta aac ggc gtt acc tac gac acg ttg aaa gac 1200 Thr Thr Leu Asp Ser Leu Asn Gly Val Thr Tyr Asp Thr Leu Lys Asp 385 390 395 400 tgg ata att tcg ggc atg cag gag tac tac agc acc ctg cag act acc 1248 Trp Ile Ile Ser Gly Met Gln Glu Tyr Tyr Ser Thr Leu Gln Thr Thr 405 410 415 tgg ccc gat ctc aca ccc ttc cac cag gct ggc ggc aaa gtg atc cac 1296 Trp Pro Asp Leu Thr Pro Phe His Gln Ala Gly Gly Lys Val Ile His 420 425 430 tac cat ggc gac gct gat ttc agc atc ccc act gct tcg tct atc cgc 1344 Tyr His Gly Asp Ala Asp Phe Ser Ile Pro Thr Ala Ser Ser Ile Arg 435 440 445 tac tgg gag tcg gtg cgg agt acc atg tac ggc aac ctg tcg tac aaa 1392 Tyr Trp Glu Ser Val Arg Ser Thr Met Tyr Gly Asn Leu Ser Tyr Lys 450 455 460 gct ggt gct aac gca ttg aat gaa tgg tac cgc tta tac act gtg cct 1440 Ala Gly Ala Asn Ala Leu Asn Glu Trp Tyr Arg Leu Tyr Thr Val Pro 465 470 475 480 ggt gcc ggc cac tgc tcg acc aac gat gcc atg ccc aat ggt cca tgg 1488 Gly Ala Gly His Cys Ser Thr Asn Asp Ala Met Pro Asn Gly Pro Trp 485 490 495 cct cag acc aac ctc gct acc atg gta gaa tgg gtc gaa aag gga gtg 1536 Pro Gln Thr Asn Leu Ala Thr Met Val Glu Trp Val Glu Lys Gly Val 500 505 510 act ccg gtc acc ctg aat gca aca gtg ctc cag ggc gag tat gaa ggc 1584 Thr Pro Val Thr Leu Asn Ala Thr Val Leu Gln Gly Glu Tyr Glu Gly 515 520 525 gag acc cag cag ctc tgc gcg tgg cca ttg cgt cct ctc tgg aag aac 1632 Glu Thr Gln Gln Leu Cys Ala Trp Pro Leu Arg Pro Leu Trp Lys Asn 530 535 540 aaa gga aag acc cta aac tgt gtg tat gac cag gcg tcc atc aac agc 1680 Lys Gly Lys Thr Leu Asn Cys Val Tyr Asp Gln Ala Ser Ile Asn Ser 545 550 555 560 tgg cac tat gac ttg gat gca gtt cct atg cct gta tat tag 1722 Trp His Tyr Asp Leu Asp Ala Val Pro Met Pro Val Tyr * 565 570 3 573 PRT Aspergillus 3 Met Arg Pro Ser Ser Cys Ile Pro Phe Ser Val Gly Leu Ala Val Val 1 5 10 15 Ala His Ala Ala Ser Pro Ser Thr Leu Glu Glu Leu Cys Thr Val Ser 20 25 30 Tyr Leu Gln Thr Val Leu Pro Ser Ser Lys Phe Ile Gln Gly Ile Thr 35 40 45 Ile Asp Ser Asp Ser Leu Thr Thr Ser Val Val Thr Asn Ser Thr Val 50 55 60 Ser Ser Val Asp Tyr Pro Thr Ala Thr Ile Asp Tyr Cys Asn Val Thr 65 70 75 80 Leu Ala Tyr Ser His Asp Gly Ile Asp Gly Asp Arg Val Leu Leu Gln 85 90 95 Ile Trp Leu Pro Ala Pro Thr Asp Phe Gln Asn Arg Trp Leu Ser Thr 100 105 110 Gly Gly Gly Gly Tyr Ala Ile Asn Ser Gly Thr Arg Met Leu Pro Glu 115 120 125 Gly Ile Ile Tyr Gly Ala Ala Ser Gly Leu Thr Asp Gly Gly Phe Gly 130 135 140 Gly Phe Ser Val Asn Ala Asp Ser Ala Met Leu Leu Ala Asn Gly Thr 145 150 155 160 Leu Asn Tyr Glu Ala Leu Tyr Met Phe Gly Tyr Lys Ala His Arg Glu 165 170 175 Leu Ser Leu Ile Gly Lys Ala Phe Thr Arg Lys Val Tyr Gly Met Ala 180 185 190 Asp Ser Glu Lys Leu Tyr Ala Tyr Tyr His Gly Cys Ser Glu Gly Gly 195 200 205 Arg Glu Gly Trp Ser Gln Val Gln Arg Tyr Gly Asp Glu Trp Asp Gly 210 215 220 Ala Ile Ile Gly Ala Pro Ala Phe Arg Trp Ser Phe Gln Gln Thr Gln 225 230 235 240 His Leu Phe Ser Asn Ile Val Glu Lys Thr Leu Asp Tyr Tyr Pro Pro 245 250 255 Pro Cys Glu Leu Glu Lys Ile Val Asn Glu Thr Ile Val Ala Cys Asp 260 265 270 Pro Leu Asp Gly Arg Thr Asp Gly Val Val Ala Arg Thr Asp Leu Cys 275 280 285 Leu Leu His Phe Asp Leu Lys His Val Ile Gly Lys Lys Tyr Ser Cys 290 295 300 Ala Ala Ser Thr Thr Ala Pro Ala Gln Ser Gly Thr Val Ser Ala Lys 305 310 315 320 Ala Val Glu Val Ala Lys Thr Ile Ile Asn Gly Leu His Asp Thr Gln 325 330 335 Gly Arg Arg Val Tyr Phe Ser Tyr Gln Pro Ser Ala Ala Phe Asp Asp 340 345 350 Ala Gln Thr Gln Phe Asn Ala Asp Thr Gly Lys Trp Glu Leu Ser Ile 355 360 365 Asn Gln Leu Gly Gly Lys His Ile Ala Leu Leu Met Asn Lys Asn Ser 370 375 380 Thr Thr Leu Asp Ser Leu Asn Gly Val Thr Tyr Asp Thr Leu Lys Asp 385 390 395 400 Trp Ile Ile Ser Gly Met Gln Glu Tyr Tyr Ser Thr Leu Gln Thr Thr 405 410 415 Trp Pro Asp Leu Thr Pro Phe His Gln Ala Gly Gly Lys Val Ile His 420 425 430 Tyr His Gly Asp Ala Asp Phe Ser Ile Pro Thr Ala Ser Ser Ile Arg 435 440 445 Tyr Trp Glu Ser Val Arg Ser Thr Met Tyr Gly Asn Leu Ser Tyr Lys 450 455 460 Ala Gly Ala Asn Ala Leu Asn Glu Trp Tyr Arg Leu Tyr Thr Val Pro 465 470 475 480 Gly Ala Gly His Cys Ser Thr Asn Asp Ala Met Pro Asn Gly Pro Trp 485 490 495 Pro Gln Thr Asn Leu Ala Thr Met Val Glu Trp Val Glu Lys Gly Val 500 505 510 Thr Pro Val Thr Leu Asn Ala Thr Val Leu Gln Gly Glu Tyr Glu Gly 515 520 525 Glu Thr Gln Gln Leu Cys Ala Trp Pro Leu Arg Pro Leu Trp Lys Asn 530 535 540 Lys Gly Lys Thr Leu Asn Cys Val Tyr Asp Gln Ala Ser Ile Asn Ser 545 550 555 560 Trp His Tyr Asp Leu Asp Ala Val Pro Met Pro Val Tyr 565 570 4 1767 DNA Aspergillus 4 atgcgtatct cctacggctc agccgttgct gctctggcag cggcagctaa tgctgcatct 60 ctcgctgacg tgtgcaccat ctcccatgtg cagtccgtgc ttccttcaaa cggaactctt 120 ctgggtatca acgtgattcc gtccgccgtg actgcaagtg cagtctacaa cagtacctcc 180 agcggcggca tgggcggcat gggcggctcc aacagtgcca actaccccta ctgcaatgtg 240 acggtcacct atacccaccc cggtaagggc gacaaggtgg tcgttaagta tgccttcccc 300 cagccttccg acttcaagaa ccgcttctac gttgccgggg gtggcggtta ctccctctcc 360 agcgatgcca ctggcggtct agagtatggt gcggcgtctg gtgccaccga tgcgggttac 420 gatgccttca gctacagcta cgacgaggtg gttctttacg gcaacggatc gatcaactgg 480 gacgccacgt acatgttcgc ctaccaggcc ctgggcgaga tgaccactct cggcaagaca 540 ttgacccgaa acttctacgg tctgtctagc gatgccaaga tctacaccta ctacgaagga 600 tgctccgacg gtggacgtga aggcatgagc caggttcagc gctacggcga tctgtacgac 660 ggtgccatca ccggtgcccc ggctttccgc tatgcccagc agcaggtcca ccacgtcttt 720 tcgtcggttg tggagaagac tctggactac taccctcccc cgtgcgaact ggccaagatc 780 gtcaacgcca ccattgaggc ctgcgatcct ctcgacggcc gcactgacgg ggtggtctcc 840 cgcaccgacc tctgcaagct gcactttgac ctttcgaaga tcatcgggga gccgtactac 900 tgcgccgcaa agaccagcac ctccctcggc ttcggcttca gcaaacgcca ggcagccggc 960 agcacgacca gctaccagcc tgcacaaaac ggcaccgtca ccaaggaggg ggtggctgtc 1020 gccaaggcca tttacgacgg tctgcacaac acccagggcc agcgcgccta cctctcctgg 1080 cagatcgcct cggaattctc cgatgccacc accgagtgga acaatgacac cggctcctgg 1140 gagctgagca tcccgtccac cggcggcgaa ttcgtgacca agttcgtcca actcctggat 1200 ctcgataacc tgtccactct cgacaacgtc acctacgaca ccctcgtcga atggatgaac 1260 accgccatgg tgcgctacat ggacagcctg cagaccaccg tcccggacct gacgactttc 1320 aaatcctccg gcggcaagct gctgcattac cacggtgaat ccgaccccag tatccccgcc 1380 gcgtcctcgg tgcactactg gcagtctgtg cgctcgatca tgtaccccgg tgtgtcggcc 1440 gcgaagagtc tgaaggagct ccaggaatgg taccagttct atctcatccc cggtgcggcg 1500 cactgcggtg ccaactccct gcagcctggc ccgtacccgc agaacaacat ggacatcatg 1560 atcgactggg tggagaacgg cgtgcagccg agccgactga acaccacagt gtcctcgggc 1620 gactacgccg gcgagaccca gatgctctgc cagtggccga cccgtcctct gtggaaggac 1680 aactcgacct ttgactgtgt caacgacgaa aagtcgatcg agagctggac ctataccttt 1740 cctgctttca aggtatctgt ctactga 1767 5 1767 DNA Aspergillus CDS (1)...(1767) 5 atg cgt atc tcc tac ggc tca gcc gtt gct gct ctg gca gcg gca gct 48 Met Arg Ile Ser Tyr Gly Ser Ala Val Ala Ala Leu Ala Ala Ala Ala 1 5 10 15 aat gct gca tct ctc gct gac gtg tgc acc atc tcc cat gtg cag tcc 96 Asn Ala Ala Ser Leu Ala Asp Val Cys Thr Ile Ser His Val Gln Ser 20 25 30 gtg ctt cct tca aac gga act ctt ctg ggt atc aac gtg att ccg tcc 144 Val Leu Pro Ser Asn Gly Thr Leu Leu Gly Ile Asn Val Ile Pro Ser 35 40 45 gcc gtg act gca agt gca gtc tac aac agt acc tcc agc ggc ggc atg 192 Ala Val Thr Ala Ser Ala Val Tyr Asn Ser Thr Ser Ser Gly Gly Met 50 55 60 ggc ggc atg ggc ggc tcc aac agt gcc aac tac ccc tac tgc aat gtg 240 Gly Gly Met Gly Gly Ser Asn Ser Ala Asn Tyr Pro Tyr Cys Asn Val 65 70 75 80 acg gtc acc tat acc cac ccc ggt aag ggc gac aag gtg gtc gtt aag 288 Thr Val Thr Tyr Thr His Pro Gly Lys Gly Asp Lys Val Val Val Lys 85 90 95 tat gcc ttc ccc cag cct tcc gac ttc aag aac cgc ttc tac gtt gcc 336 Tyr Ala Phe Pro Gln Pro Ser Asp Phe Lys Asn Arg Phe Tyr Val Ala 100 105 110 ggg ggt ggc ggt tac tcc ctc tcc agc gat gcc act ggc ggt cta gag 384 Gly Gly Gly Gly Tyr Ser Leu Ser Ser Asp Ala Thr Gly Gly Leu Glu 115 120 125 tat ggt gcg gcg tct ggt gcc acc gat gcg ggt tac gat gcc ttc agc 432 Tyr Gly Ala Ala Ser Gly Ala Thr Asp Ala Gly Tyr Asp Ala Phe Ser 130 135 140 tac agc tac gac gag gtg gtt ctt tac ggc aac gga tcg atc aac tgg 480 Tyr Ser Tyr Asp Glu Val Val Leu Tyr Gly Asn Gly Ser Ile Asn Trp 145 150 155 160 gac gcc acg tac atg ttc gcc tac cag gcc ctg ggc gag atg acc act 528 Asp Ala Thr Tyr Met Phe Ala Tyr Gln Ala Leu Gly Glu Met Thr Thr 165 170 175 ctc ggc aag aca ttg acc cga aac ttc tac ggt ctg tct agc gat gcc 576 Leu Gly Lys Thr Leu Thr Arg Asn Phe Tyr Gly Leu Ser Ser Asp Ala 180 185 190 aag atc tac acc tac tac gaa gga tgc tcc gac ggt gga cgt gaa ggc 624 Lys Ile Tyr Thr Tyr Tyr Glu Gly Cys Ser Asp Gly Gly Arg Glu Gly 195 200 205 atg agc cag gtt cag cgc tac ggc gat ctg tac gac ggt gcc atc acc 672 Met Ser Gln Val Gln Arg Tyr Gly Asp Leu Tyr Asp Gly Ala Ile Thr 210 215 220 ggt gcc ccg gct ttc cgc tat gcc cag cag cag gtc cac cac gtc ttt 720 Gly Ala Pro Ala Phe Arg Tyr Ala Gln Gln Gln Val His His Val Phe 225 230 235 240 tcg tcg gtt gtg gag aag act ctg gac tac tac cct ccc ccg tgc gaa 768 Ser Ser Val Val Glu Lys Thr Leu Asp Tyr Tyr Pro Pro Pro Cys Glu 245 250 255 ctg gcc aag atc gtc aac gcc acc att gag gcc tgc gat cct ctc gac 816 Leu Ala Lys Ile Val Asn Ala Thr Ile Glu Ala Cys Asp Pro Leu Asp 260 265 270 ggc cgc act gac ggg gtg gtc tcc cgc acc gac ctc tgc aag ctg cac 864 Gly Arg Thr Asp Gly Val Val Ser Arg Thr Asp Leu Cys Lys Leu His 275 280 285 ttt gac ctt tcg aag atc atc ggg gag ccg tac tac tgc gcc gca aag 912 Phe Asp Leu Ser Lys Ile Ile Gly Glu Pro Tyr Tyr Cys Ala Ala Lys 290 295 300 acc agc acc tcc ctc ggc ttc ggc ttc agc aaa cgc cag gca gcc ggc 960 Thr Ser Thr Ser Leu Gly Phe Gly Phe Ser Lys Arg Gln Ala Ala Gly 305 310 315 320 agc acg acc agc tac cag cct gca caa aac ggc acc gtc acc aag gag 1008 Ser Thr Thr Ser Tyr Gln Pro Ala Gln Asn Gly Thr Val Thr Lys Glu 325 330 335 ggg gtg gct gtc gcc aag gcc att tac gac ggt ctg cac aac acc cag 1056 Gly Val Ala Val Ala Lys Ala Ile Tyr Asp Gly Leu His Asn Thr Gln 340 345 350 ggc cag cgc gcc tac ctc tcc tgg cag atc gcc tcg gaa ttc tcc gat 1104 Gly Gln Arg Ala Tyr Leu Ser Trp Gln Ile Ala Ser Glu Phe Ser Asp 355 360 365 gcc acc acc gag tgg aac aat gac acc ggc tcc tgg gag ctg agc atc 1152 Ala Thr Thr Glu Trp Asn Asn Asp Thr Gly Ser Trp Glu Leu Ser Ile 370 375 380 ccg tcc acc ggc ggc gaa ttc gtg acc aag ttc gtc caa ctc ctg gat 1200 Pro Ser Thr Gly Gly Glu Phe Val Thr Lys Phe Val Gln Leu Leu Asp 385 390 395 400 ctc gat aac ctg tcc act ctc gac aac gtc acc tac gac acc ctc gtc 1248 Leu Asp Asn Leu Ser Thr Leu Asp Asn Val Thr Tyr Asp Thr Leu Val 405 410 415 gaa tgg atg aac acc gcc atg gtg cgc tac atg gac agc ctg cag acc 1296 Glu Trp Met Asn Thr Ala Met Val Arg Tyr Met Asp Ser Leu Gln Thr 420 425 430 acc gtc ccg gac ctg acg act ttc aaa tcc tcc ggc ggc aag ctg ctg 1344 Thr Val Pro Asp Leu Thr Thr Phe Lys Ser Ser Gly Gly Lys Leu Leu 435 440 445 cat tac cac ggt gaa tcc gac ccc agt atc ccc gcc gcg tcc tcg gtg 1392 His Tyr His Gly Glu Ser Asp Pro Ser Ile Pro Ala Ala Ser Ser Val 450 455 460 cac tac tgg cag tct gtg cgc tcg atc atg tac ccc ggt gtg tcg gcc 1440 His Tyr Trp Gln Ser Val Arg Ser Ile Met Tyr Pro Gly Val Ser Ala 465 470 475 480 gcg aag agt ctg aag gag ctc cag gaa tgg tac cag ttc tat ctc atc 1488 Ala Lys Ser Leu Lys Glu Leu Gln Glu Trp Tyr Gln Phe Tyr Leu Ile 485 490 495 ccc ggt gcg gcg cac tgc ggt gcc aac tcc ctg cag cct ggc ccg tac 1536 Pro Gly Ala Ala His Cys Gly Ala Asn Ser Leu Gln Pro Gly Pro Tyr 500 505 510 ccg cag aac aac atg gac atc atg atc gac tgg gtg gag aac ggc gtg 1584 Pro Gln Asn Asn Met Asp Ile Met Ile Asp Trp Val Glu Asn Gly Val 515 520 525 cag ccg agc cga ctg aac acc aca gtg tcc tcg ggc gac tac gcc ggc 1632 Gln Pro Ser Arg Leu Asn Thr Thr Val Ser Ser Gly Asp Tyr Ala Gly 530 535 540 gag acc cag atg ctc tgc cag tgg ccg acc cgt cct ctg tgg aag gac 1680 Glu Thr Gln Met Leu Cys Gln Trp Pro Thr Arg Pro Leu Trp Lys Asp 545 550 555 560 aac tcg acc ttt gac tgt gtc aac gac gaa aag tcg atc gag agc tgg 1728 Asn Ser Thr Phe Asp Cys Val Asn Asp Glu Lys Ser Ile Glu Ser Trp 565 570 575 acc tat acc ttt cct gct ttc aag gta tct gtc tac tga 1767 Thr Tyr Thr Phe Pro Ala Phe Lys Val Ser Val Tyr * 580 585 6 588 PRT Aspergillus 6 Met Arg Ile Ser Tyr Gly Ser Ala Val Ala Ala Leu Ala Ala Ala Ala 1 5 10 15 Asn Ala Ala Ser Leu Ala Asp Val Cys Thr Ile Ser His Val Gln Ser 20 25 30 Val Leu Pro Ser Asn Gly Thr Leu Leu Gly Ile Asn Val Ile Pro Ser 35 40 45 Ala Val Thr Ala Ser Ala Val Tyr Asn Ser Thr Ser Ser Gly Gly Met 50 55 60 Gly Gly Met Gly Gly Ser Asn Ser Ala Asn Tyr Pro Tyr Cys Asn Val 65 70 75 80 Thr Val Thr Tyr Thr His Pro Gly Lys Gly Asp Lys Val Val Val Lys 85 90 95 Tyr Ala Phe Pro Gln Pro Ser Asp Phe Lys Asn Arg Phe Tyr Val Ala 100 105 110 Gly Gly Gly Gly Tyr Ser Leu Ser Ser Asp Ala Thr Gly Gly Leu Glu 115 120 125 Tyr Gly Ala Ala Ser Gly Ala Thr Asp Ala Gly Tyr Asp Ala Phe Ser 130 135 140 Tyr Ser Tyr Asp Glu Val Val Leu Tyr Gly Asn Gly Ser Ile Asn Trp 145 150 155 160 Asp Ala Thr Tyr Met Phe Ala Tyr Gln Ala Leu Gly Glu Met Thr Thr 165 170 175 Leu Gly Lys Thr Leu Thr Arg Asn Phe Tyr Gly Leu Ser Ser Asp Ala 180 185 190 Lys Ile Tyr Thr Tyr Tyr Glu Gly Cys Ser Asp Gly Gly Arg Glu Gly 195 200 205 Met Ser Gln Val Gln Arg Tyr Gly Asp Leu Tyr Asp Gly Ala Ile Thr 210 215 220 Gly Ala Pro Ala Phe Arg Tyr Ala Gln Gln Gln Val His His Val Phe 225 230 235 240 Ser Ser Val Val Glu Lys Thr Leu Asp Tyr Tyr Pro Pro Pro Cys Glu 245 250 255 Leu Ala Lys Ile Val Asn Ala Thr Ile Glu Ala Cys Asp Pro Leu Asp 260 265 270 Gly Arg Thr Asp Gly Val Val Ser Arg Thr Asp Leu Cys Lys Leu His 275 280 285 Phe Asp Leu Ser Lys Ile Ile Gly Glu Pro Tyr Tyr Cys Ala Ala Lys 290 295 300 Thr Ser Thr Ser Leu Gly Phe Gly Phe Ser Lys Arg Gln Ala Ala Gly 305 310 315 320 Ser Thr Thr Ser Tyr Gln Pro Ala Gln Asn Gly Thr Val Thr Lys Glu 325 330 335 Gly Val Ala Val Ala Lys Ala Ile Tyr Asp Gly Leu His Asn Thr Gln 340 345 350 Gly Gln Arg Ala Tyr Leu Ser Trp Gln Ile Ala Ser Glu Phe Ser Asp 355 360 365 Ala Thr Thr Glu Trp Asn Asn Asp Thr Gly Ser Trp Glu Leu Ser Ile 370 375 380 Pro Ser Thr Gly Gly Glu Phe Val Thr Lys Phe Val Gln Leu Leu Asp 385 390 395 400 Leu Asp Asn Leu Ser Thr Leu Asp Asn Val Thr Tyr Asp Thr Leu Val 405 410 415 Glu Trp Met Asn Thr Ala Met Val Arg Tyr Met Asp Ser Leu Gln Thr 420 425 430 Thr Val Pro Asp Leu Thr Thr Phe Lys Ser Ser Gly Gly Lys Leu Leu 435 440 445 His Tyr His Gly Glu Ser Asp Pro Ser Ile Pro Ala Ala Ser Ser Val 450 455 460 His Tyr Trp Gln Ser Val Arg Ser Ile Met Tyr Pro Gly Val Ser Ala 465 470 475 480 Ala Lys Ser Leu Lys Glu Leu Gln Glu Trp Tyr Gln Phe Tyr Leu Ile 485 490 495 Pro Gly Ala Ala His Cys Gly Ala Asn Ser Leu Gln Pro Gly Pro Tyr 500 505 510 Pro Gln Asn Asn Met Asp Ile Met Ile Asp Trp Val Glu Asn Gly Val 515 520 525 Gln Pro Ser Arg Leu Asn Thr Thr Val Ser Ser Gly Asp Tyr Ala Gly 530 535 540 Glu Thr Gln Met Leu Cys Gln Trp Pro Thr Arg Pro Leu Trp Lys Asp 545 550 555 560 Asn Ser Thr Phe Asp Cys Val Asn Asp Glu Lys Ser Ile Glu Ser Trp 565 570 575 Thr Tyr Thr Phe Pro Ala Phe Lys Val Ser Val Tyr 580 585 7 1713 DNA Aspergillus 7 atgaagcacc ttgcatcttc catcgcattg actctactgt tgcctgccgt gcaggcccag 60 cagaccgtat ggggccaatg tatgttctgg ctgtcactgg aataagactg tatcaactgc 120 tgatatgctt ctaggtggcg gccaaggctg gtctggcccg acgagctgtg ttgccggcgc 180 agcctgtagc acactgaatc cctgtatgtt agatatcgtc ctgagtggag acttatactg 240 acttccttag actacgctca gtgtatcccg ggagccaccg cgacgtccac caccctcacg 300 acgacgacgg cggcgacgac gacatcccag accaccacca aacctaccac gactggtcca 360 actacatccg cacccaccgt gaccgcatcc ggtaaccctt tcagcggcta ccagctgtat 420 gccaacccct actactcctc cgaggtccat actctggcca tgccttctct gcccagctcg 480 ctgcagccca aggctagtgc tgttgctgaa gtgccctcat ttgtttggct gtaagtggcc 540 ttatcccaat actgagacca actctctgac agtcgtagcg acgttgccgc caaggtgccc 600 actatgggaa cctacctggc cgacattcag gccaagaaca aggccggcgc caaccctcct 660 atcgctggta tcttcgtggt ctacgacttg ccggaccgtg actgcgccgc tctggccagt 720 aatggcgagt actcaattgc caacaacggt gtggccaact acaaggcgta cattgacgcc 780 atccgtgctc agctggtgaa gtactctgac gttcacacca tcctcgtcat cggtaggccg 840 tacacctccg ttgcgcgccg cctttctctg acatcttgca gaacccgaca gcttggccaa 900 cctggtgacc aacctcaacg tcgccaaatg cgccaatgcg cagagcgcct acctggagtg 960 tgtcgactat gctctgaagc agctcaacct gcccaacgtc gccatgtacc tcgacgcagg 1020 tatgcctcac ttcccgcatt ctgtatccct tccagacact aactcatcag gccatgcggg 1080 ctggctcgga tggcccgcca acttgggccc cgccgcaaca ctcttcgcca aagtctacac 1140 cgacgcgggt tcccccgcgg ctgttcgtgg cctggccacc aacgtcgcca actacaacgc 1200 ctggtcgctc agtacctgcc cctcctacac ccagggagac cccaactgcg acgagaagaa 1260 gtacatcaac gccatggcgc ctcttctcaa ggaagccggc ttcgatgccc acttcatcat 1320 ggatacctgt aagtgcttat tccaatcgcc gatgtgtgcc gactaatcaa tgtttcagcc 1380 cggaatggcg tccagcccac gaagcaaaac gcctggggtg actggtgcaa cgtcatcggc 1440 accggcttcg gtgttcgccc ctcgactaac accggcgatc cgctccagga tgcctttgta 1500 tggatcaagc ccggtggaga gagtgatggc acgtccaact cgacttcccc ccggtatgac 1560 gcgcactgcg gatatagtga tgctctgcag cctgctcctg aggctggtac ttggttccag 1620 gtatgtcatc cattagccag atgagggata agtgactgac ggacctaggc ctactttgag 1680 cagcttctga ccaacgctaa cccgtccttt taa 1713 8 1365 DNA Aspergillus CDS (1)...(1365) 8 atg aag cac ctt gca tct tcc atc gca ttg act cta ctg ttg cct gcc 48 Met Lys His Leu Ala Ser Ser Ile Ala Leu Thr Leu Leu Leu Pro Ala 1 5 10 15 gtg cag gcc cag cag acc gta tgg ggc caa tgt ggc ggc caa ggc tgg 96 Val Gln Ala Gln Gln Thr Val Trp Gly Gln Cys Gly Gly Gln Gly Trp 20 25 30 tct ggc ccg acg agc tgt gtt gcc ggc gca gcc tgt agc aca ctg aat 144 Ser Gly Pro Thr Ser Cys Val Ala Gly Ala Ala Cys Ser Thr Leu Asn 35 40 45 ccc tac tac gct cag tgt atc ccg gga gcc acc gcg acg tcc acc acc 192 Pro Tyr Tyr Ala Gln Cys Ile Pro Gly Ala Thr Ala Thr Ser Thr Thr 50 55 60 ctc acg acg acg acg gcg gcg acg acg aca tcc cag acc acc acc aaa 240 Leu Thr Thr Thr Thr Ala Ala Thr Thr Thr Ser Gln Thr Thr Thr Lys 65 70 75 80 cct acc acg act ggt cca act aca tcc gca ccc acc gtg acc gca tcc 288 Pro Thr Thr Thr Gly Pro Thr Thr Ser Ala Pro Thr Val Thr Ala Ser 85 90 95 ggt aac cct ttc agc ggc tac cag ctg tat gcc aac ccc tac tac tcc 336 Gly Asn Pro Phe Ser Gly Tyr Gln Leu Tyr Ala Asn Pro Tyr Tyr Ser 100 105 110 tcc gag gtc cat act ctg gcc atg cct tct ctg ccc agc tcg ctg cag 384 Ser Glu Val His Thr Leu Ala Met Pro Ser Leu Pro Ser Ser Leu Gln 115 120 125 ccc aag gct agt gct gtt gct gaa gtg ccc tca ttt gtt tgg ctc gac 432 Pro Lys Ala Ser Ala Val Ala Glu Val Pro Ser Phe Val Trp Leu Asp 130 135 140 gtt gcc gcc aag gtg ccc act atg gga acc tac ctg gcc gac att cag 480 Val Ala Ala Lys Val Pro Thr Met Gly Thr Tyr Leu Ala Asp Ile Gln 145 150 155 160 gcc aag aac aag gcc ggc gcc aac cct cct atc gct ggt atc ttc gtg 528 Ala Lys Asn Lys Ala Gly Ala Asn Pro Pro Ile Ala Gly Ile Phe Val 165 170 175 gtc tac gac ttg ccg gac cgt gac tgc gcc gct ctg gcc agt aat ggc 576 Val Tyr Asp Leu Pro Asp Arg Asp Cys Ala Ala Leu Ala Ser Asn Gly 180 185 190 gag tac tca att gcc aac aac ggt gtg gcc aac tac aag gcg tac att 624 Glu Tyr Ser Ile Ala Asn Asn Gly Val Ala Asn Tyr Lys Ala Tyr Ile 195 200 205 gac gcc atc cgt gct cag ctg gtg aag tac tct gac gtt cac acc atc 672 Asp Ala Ile Arg Ala Gln Leu Val Lys Tyr Ser Asp Val His Thr Ile 210 215 220 ctc gtc atc gaa ccc gac agc ttg gcc aac ctg gtg acc aac ctc aac 720 Leu Val Ile Glu Pro Asp Ser Leu Ala Asn Leu Val Thr Asn Leu Asn 225 230 235 240 gtc gcc aaa tgc gcc aat gcg cag agc gcc tac ctg gag tgt gtc gac 768 Val Ala Lys Cys Ala Asn Ala Gln Ser Ala Tyr Leu Glu Cys Val Asp 245 250 255 tat gct ctg aag cag ctc aac ctg ccc aac gtc gcc atg tac ctc gac 816 Tyr Ala Leu Lys Gln Leu Asn Leu Pro Asn Val Ala Met Tyr Leu Asp 260 265 270 gca ggc cat gcg ggc tgg ctc gga tgg ccc gcc aac ttg ggc ccc gcc 864 Ala Gly His Ala Gly Trp Leu Gly Trp Pro Ala Asn Leu Gly Pro Ala 275 280 285 gca aca ctc ttc gcc aaa gtc tac acc gac gcg ggt tcc ccc gcg gct 912 Ala Thr Leu Phe Ala Lys Val Tyr Thr Asp Ala Gly Ser Pro Ala Ala 290 295 300 gtt cgt ggc ctg gcc acc aac gtc gcc aac tac aac gcc tgg tcg ctc 960 Val Arg Gly Leu Ala Thr Asn Val Ala Asn Tyr Asn Ala Trp Ser Leu 305 310 315 320 agt acc tgc ccc tcc tac acc cag gga gac ccc aac tgc gac gag aag 1008 Ser Thr Cys Pro Ser Tyr Thr Gln Gly Asp Pro Asn Cys Asp Glu Lys 325 330 335 aag tac atc aac gcc atg gcg cct ctt ctc aag gaa gcc ggc ttc gat 1056 Lys Tyr Ile Asn Ala Met Ala Pro Leu Leu Lys Glu Ala Gly Phe Asp 340 345 350 gcc cac ttc atc atg gat acc tcc cgg aat ggc gtc cag ccc acg aag 1104 Ala His Phe Ile Met Asp Thr Ser Arg Asn Gly Val Gln Pro Thr Lys 355 360 365 caa aac gcc tgg ggt gac tgg tgc aac gtc atc ggc acc ggc ttc ggt 1152 Gln Asn Ala Trp Gly Asp Trp Cys Asn Val Ile Gly Thr Gly Phe Gly 370 375 380 gtt cgc ccc tcg act aac acc ggc gat ccg ctc cag gat gcc ttt gta 1200 Val Arg Pro Ser Thr Asn Thr Gly Asp Pro Leu Gln Asp Ala Phe Val 385 390 395 400 tgg atc aag ccc ggt gga gag agt gat ggc acg tcc aac tcg act tcc 1248 Trp Ile Lys Pro Gly Gly Glu Ser Asp Gly Thr Ser Asn Ser Thr Ser 405 410 415 ccc cgg tat gac gcg cac tgc gga tat agt gat gct ctg cag cct gct 1296 Pro Arg Tyr Asp Ala His Cys Gly Tyr Ser Asp Ala Leu Gln Pro Ala 420 425 430 cct gag gct ggt act tgg ttc cag gcc tac ttt gag cag ctt ctg acc 1344 Pro Glu Ala Gly Thr Trp Phe Gln Ala Tyr Phe Glu Gln Leu Leu Thr 435 440 445 aac gct aac ccg tcc ttt taa 1365 Asn Ala Asn Pro Ser Phe * 450 9 454 PRT Aspergillus 9 Met Lys His Leu Ala Ser Ser Ile Ala Leu Thr Leu Leu Leu Pro Ala 1 5 10 15 Val Gln Ala Gln Gln Thr Val Trp Gly Gln Cys Gly Gly Gln Gly Trp 20 25 30 Ser Gly Pro Thr Ser Cys Val Ala Gly Ala Ala Cys Ser Thr Leu Asn 35 40 45 Pro Tyr Tyr Ala Gln Cys Ile Pro Gly Ala Thr Ala Thr Ser Thr Thr 50 55 60 Leu Thr Thr Thr Thr Ala Ala Thr Thr Thr Ser Gln Thr Thr Thr Lys 65 70 75 80 Pro Thr Thr Thr Gly Pro Thr Thr Ser Ala Pro Thr Val Thr Ala Ser 85 90 95 Gly Asn Pro Phe Ser Gly Tyr Gln Leu Tyr Ala Asn Pro Tyr Tyr Ser 100 105 110 Ser Glu Val His Thr Leu Ala Met Pro Ser Leu Pro Ser Ser Leu Gln 115 120 125 Pro Lys Ala Ser Ala Val Ala Glu Val Pro Ser Phe Val Trp Leu Asp 130 135 140 Val Ala Ala Lys Val Pro Thr Met Gly Thr Tyr Leu Ala Asp Ile Gln 145 150 155 160 Ala Lys Asn Lys Ala Gly Ala Asn Pro Pro Ile Ala Gly Ile Phe Val 165 170 175 Val Tyr Asp Leu Pro Asp Arg Asp Cys Ala Ala Leu Ala Ser Asn Gly 180 185 190 Glu Tyr Ser Ile Ala Asn Asn Gly Val Ala Asn Tyr Lys Ala Tyr Ile 195 200 205 Asp Ala Ile Arg Ala Gln Leu Val Lys Tyr Ser Asp Val His Thr Ile 210 215 220 Leu Val Ile Glu Pro Asp Ser Leu Ala Asn Leu Val Thr Asn Leu Asn 225 230 235 240 Val Ala Lys Cys Ala Asn Ala Gln Ser Ala Tyr Leu Glu Cys Val Asp 245 250 255 Tyr Ala Leu Lys Gln Leu Asn Leu Pro Asn Val Ala Met Tyr Leu Asp 260 265 270 Ala Gly His Ala Gly Trp Leu Gly Trp Pro Ala Asn Leu Gly Pro Ala 275 280 285 Ala Thr Leu Phe Ala Lys Val Tyr Thr Asp Ala Gly Ser Pro Ala Ala 290 295 300 Val Arg Gly Leu Ala Thr Asn Val Ala Asn Tyr Asn Ala Trp Ser Leu 305 310 315 320 Ser Thr Cys Pro Ser Tyr Thr Gln Gly Asp Pro Asn Cys Asp Glu Lys 325 330 335 Lys Tyr Ile Asn Ala Met Ala Pro Leu Leu Lys Glu Ala Gly Phe Asp 340 345 350 Ala His Phe Ile Met Asp Thr Ser Arg Asn Gly Val Gln Pro Thr Lys 355 360 365 Gln Asn Ala Trp Gly Asp Trp Cys Asn Val Ile Gly Thr Gly Phe Gly 370 375 380 Val Arg Pro Ser Thr Asn Thr Gly Asp Pro Leu Gln Asp Ala Phe Val 385 390 395 400 Trp Ile Lys Pro Gly Gly Glu Ser Asp Gly Thr Ser Asn Ser Thr Ser 405 410 415 Pro Arg Tyr Asp Ala His Cys Gly Tyr Ser Asp Ala Leu Gln Pro Ala 420 425 430 Pro Glu Ala Gly Thr Trp Phe Gln Ala Tyr Phe Glu Gln Leu Leu Thr 435 440 445 Asn Ala Asn Pro Ser Phe 450 10 1866 DNA Aspergillus 10 atgaccgaat acgactatat cattgtcggc gcaggcatcg gtggcctggt gctggccaac 60 cgcctgagcg cagacgcctc tgtcaatgtc cttctcatcg aagccggggc caatcgcatg 120 ggcgatcctc gtatcgacac ccctgggttt ctgggcatgt tgtacggaaa cccagacttc 180 gactgggatt atatgagtgt ccctcaggta tcacctctct tccactgctc catttacggc 240 aacaatgcaa caatgctgat cgtatagccg catgtcaaca accgacaaat cgcgcagccc 300 cgcggccggg tcgtcggcgg ttcctcggcc ctgaatttct cggtcgtcct gtaccctccc 360 gcatcagact tcgaggcatg gaaggcgttg ggaaaccaag gctggggcgc agaggatatg 420 gcgccgtacc tgcggaagtt tcacacgttc tccccgccca gcaagtccac ggccgacctt 480 ctcggcgtcg atagctacat gaaagccagc agccaggggt gtgacggccc tgtgcctgtt 540 tccctgccgg acgtatatgg gccgttcaac gaagcgtggg ataagacgtt tgagaagctt 600 ggttggcgga cggacgcgga tcccatcgcc ggacgcaaac tgggtgcgtt caccccgccg 660 ctgaccgttg acgcaaagac agggaagcgg gggtatgcag cggcctacta ctcccccgag 720 gtggccgcac ggccaaacct gcgcctgctg gcagagacca tggtcgagcg ggtgctgttg 780 accaggcagg atggagacgt gctggccacc ggcgtgctgg tcaaggacaa ggatggcgcg 840 agagagattc acgcaaagaa agaagtcatt atctgcgccg gcagcctgaa tacgcctcag 900 atcctggaac tctccggcat tggaaatgca gggctgctac agaagcacga catccccgtg 960 gtgatcgaca accccggcgt tggcgagaac ctccaagatc actgcatcag ctgcatcagc 1020 ttcgagatcg ccgacggtca agtctcgggc gacattctcc gtgaccccaa cgtggtacag 1080 gccctcgtca agctgtacga ggagactcgc ggcggcccgc tggcaggcat gcccatcagc 1140 gtggcgtacc ttcctttcgt tgacggacga ggcgtcgtcc cgcggccaga agtcgaggag 1200 ctgctggcca agtatctcga cagcgccgcc cttccaccca atctgcaggc gcagtacgcg 1260 cacctcagga aagcgatcct cgacaacgat accccgtcgt cagagtacct cttcctcccc 1320 gcgcagctac acatgaaacc cggtgcgaca agcttgcccg acgtcctggc caagcccctg 1380 ccggagaact acatcagcat catgatcctg cacaaccacc ctttctcacg aggatcggtg 1440 catatctcct cccccaaggc ggaggacaaa ccgatctacg atccgaactt tctctcccac 1500 ccgctggact tggagatact cgctcggcac acgcaattcc ttgagacaat cgccgccacg 1560 gagccgttca agtctcttct caaggaacgg cggatcccgg aaaacgcgag ggacttgggc 1620 gatctggagc gagccaagga gctggtcaag gaccggctgt ttacgtgctt tcaccctgcg 1680 gggacgtgtg ccatgttgcc gcgggagatg gggggtgtgg tggatgacca gctgagagtg 1740 tatgggacac gcaatctgag ggtggttgat gccagtgtct ttccgctgga gccggcgggg 1800 aatatccagg cgacggtgta tgcggtggcg gagcgcgcag ctgatttgat catcggcagt 1860 aattag 1866 11 1806 DNA Aspergillus CDS (1)...(1806) 11 atg acc gaa tac gac tat atc att gtc ggc gca ggc atc ggt ggc ctg 48 Met Thr Glu Tyr Asp Tyr Ile Ile Val Gly Ala Gly Ile Gly Gly Leu 1 5 10 15 gtg ctg gcc aac cgc ctg agc gca gac gcc tct gtc aat gtc ctt ctc 96 Val Leu Ala Asn Arg Leu Ser Ala Asp Ala Ser Val Asn Val Leu Leu 20 25 30 atc gaa gcc ggg gcc aat cgc atg ggc gat cct cgt atc gac acc cct 144 Ile Glu Ala Gly Ala Asn Arg Met Gly Asp Pro Arg Ile Asp Thr Pro 35 40 45 ggg ttt ctg ggc atg ttg tac gga aac cca gac ttc gac tgg gat tat 192 Gly Phe Leu Gly Met Leu Tyr Gly Asn Pro Asp Phe Asp Trp Asp Tyr 50 55 60 atg agt gtc cct cag ccg cat gtc aac aac cga caa atc gcg cag ccc 240 Met Ser Val Pro Gln Pro His Val Asn Asn Arg Gln Ile Ala Gln Pro 65 70 75 80 cgc ggc cgg gtc gtc ggc ggt tcc tcg gcc ctg aat ttc tcg gtc gtc 288 Arg Gly Arg Val Val Gly Gly Ser Ser Ala Leu Asn Phe Ser Val Val 85 90 95 ctg tac cct ccc gca tca gac ttc gag gca tgg aag gcg ttg gga aac 336 Leu Tyr Pro Pro Ala Ser Asp Phe Glu Ala Trp Lys Ala Leu Gly Asn 100 105 110 caa ggc tgg ggc gca gag gat atg gcg ccg tac ctg cgg aag ttt cac 384 Gln Gly Trp Gly Ala Glu Asp Met Ala Pro Tyr Leu Arg Lys Phe His 115 120 125 acg ttc tcc ccg ccc agc aag tcc acg gcc gac ctt ctc ggc gtc gat 432 Thr Phe Ser Pro Pro Ser Lys Ser Thr Ala Asp Leu Leu Gly Val Asp 130 135 140 agc tac atg aaa gcc agc agc cag ggg tgt gac ggc cct gtg cct gtt 480 Ser Tyr Met Lys Ala Ser Ser Gln Gly Cys Asp Gly Pro Val Pro Val 145 150 155 160 tcc ctg ccg gac gta tat ggg ccg ttc aac gaa gcg tgg gat aag acg 528 Ser Leu Pro Asp Val Tyr Gly Pro Phe Asn Glu Ala Trp Asp Lys Thr 165 170 175 ttt gag aag ctt ggt tgg cgg acg gac gcg gat ccc atc gcc gga cgc 576 Phe Glu Lys Leu Gly Trp Arg Thr Asp Ala Asp Pro Ile Ala Gly Arg 180 185 190 aaa ctg ggt gcg ttc acc ccg ccg ctg acc gtt gac gca aag aca ggg 624 Lys Leu Gly Ala Phe Thr Pro Pro Leu Thr Val Asp Ala Lys Thr Gly 195 200 205 aag cgg ggg tat gca gcg gcc tac tac tcc ccc gag gtg gcc gca cgg 672 Lys Arg Gly Tyr Ala Ala Ala Tyr Tyr Ser Pro Glu Val Ala Ala Arg 210 215 220 cca aac ctg cgc ctg ctg gca gag acc atg gtc gag cgg gtg ctg ttg 720 Pro Asn Leu Arg Leu Leu Ala Glu Thr Met Val Glu Arg Val Leu Leu 225 230 235 240 acc agg cag gat gga gac gtg ctg gcc acc ggc gtg ctg gtc aag gac 768 Thr Arg Gln Asp Gly Asp Val Leu Ala Thr Gly Val Leu Val Lys Asp 245 250 255 aag gat ggc gcg aga gag att cac gca aag aaa gaa gtc att atc tgc 816 Lys Asp Gly Ala Arg Glu Ile His Ala Lys Lys Glu Val Ile Ile Cys 260 265 270 gcc ggc agc ctg aat acg cct cag atc ctg gaa ctc tcc ggc att gga 864 Ala Gly Ser Leu Asn Thr Pro Gln Ile Leu Glu Leu Ser Gly Ile Gly 275 280 285 aat gca ggg ctg cta cag aag cac gac atc ccc gtg gtg atc gac aac 912 Asn Ala Gly Leu Leu Gln Lys His Asp Ile Pro Val Val Ile Asp Asn 290 295 300 ccc ggc gtt ggc gag aac ctc caa gat cac tgc atc agc tgc atc agc 960 Pro Gly Val Gly Glu Asn Leu Gln Asp His Cys Ile Ser Cys Ile Ser 305 310 315 320 ttc gag atc gcc gac ggt caa gtc tcg ggc gac att ctc cgt gac ccc 1008 Phe Glu Ile Ala Asp Gly Gln Val Ser Gly Asp Ile Leu Arg Asp Pro 325 330 335 aac gtg gta cag gcc ctc gtc aag ctg tac gag gag act cgc ggc ggc 1056 Asn Val Val Gln Ala Leu Val Lys Leu Tyr Glu Glu Thr Arg Gly Gly 340 345 350 ccg ctg gca ggc atg ccc atc agc gtg gcg tac ctt cct ttc gtt gac 1104 Pro Leu Ala Gly Met Pro Ile Ser Val Ala Tyr Leu Pro Phe Val Asp 355 360 365 gga cga ggc gtc gtc ccg cgg cca gaa gtc gag gag ctg ctg gcc aag 1152 Gly Arg Gly Val Val Pro Arg Pro Glu Val Glu Glu Leu Leu Ala Lys 370 375 380 tat ctc gac agc gcc gcc ctt cca ccc aat ctg cag gcg cag tac gcg 1200 Tyr Leu Asp Ser Ala Ala Leu Pro Pro Asn Leu Gln Ala Gln Tyr Ala 385 390 395 400 cac ctc agg aaa gcg atc ctc gac aac gat acc ccg tcg tca gag tac 1248 His Leu Arg Lys Ala Ile Leu Asp Asn Asp Thr Pro Ser Ser Glu Tyr 405 410 415 ctc ttc ctc ccc gcg cag cta cac atg aaa ccc ggt gcg aca agc ttg 1296 Leu Phe Leu Pro Ala Gln Leu His Met Lys Pro Gly Ala Thr Ser Leu 420 425 430 ccc gac gtc ctg gcc aag ccc ctg ccg gag aac tac atc agc atc atg 1344 Pro Asp Val Leu Ala Lys Pro Leu Pro Glu Asn Tyr Ile Ser Ile Met 435 440 445 atc ctg cac aac cac cct ttc tca cga gga tcg gtg cat atc tcc tcc 1392 Ile Leu His Asn His Pro Phe Ser Arg Gly Ser Val His Ile Ser Ser 450 455 460 ccc aag gcg gag gac aaa ccg atc tac gat ccg aac ttt ctc tcc cac 1440 Pro Lys Ala Glu Asp Lys Pro Ile Tyr Asp Pro Asn Phe Leu Ser His 465 470 475 480 ccg ctg gac ttg gag ata ctc gct cgg cac acg caa ttc ctt gag aca 1488 Pro Leu Asp Leu Glu Ile Leu Ala Arg His Thr Gln Phe Leu Glu Thr 485 490 495 atc gcc gcc acg gag ccg ttc aag tct ctt ctc aag gaa cgg cgg atc 1536 Ile Ala Ala Thr Glu Pro Phe Lys Ser Leu Leu Lys Glu Arg Arg Ile 500 505 510 ccg gaa aac gcg agg gac ttg ggc gat ctg gag cga gcc aag gag ctg 1584 Pro Glu Asn Ala Arg Asp Leu Gly Asp Leu Glu Arg Ala Lys Glu Leu 515 520 525 gtc aag gac cgg ctg ttt acg tgc ttt cac cct gcg ggg acg tgt gcc 1632 Val Lys Asp Arg Leu Phe Thr Cys Phe His Pro Ala Gly Thr Cys Ala 530 535 540 atg ttg ccg cgg gag atg ggg ggt gtg gtg gat gac cag ctg aga gtg 1680 Met Leu Pro Arg Glu Met Gly Gly Val Val Asp Asp Gln Leu Arg Val 545 550 555 560 tat ggg aca cgc aat ctg agg gtg gtt gat gcc agt gtc ttt ccg ctg 1728 Tyr Gly Thr Arg Asn Leu Arg Val Val Asp Ala Ser Val Phe Pro Leu 565 570 575 gag ccg gcg ggg aat atc cag gcg acg gtg tat gcg gtg gcg gag cgc 1776 Glu Pro Ala Gly Asn Ile Gln Ala Thr Val Tyr Ala Val Ala Glu Arg 580 585 590 gca gct gat ttg atc atc ggc agt aat tag 1806 Ala Ala Asp Leu Ile Ile Gly Ser Asn * 595 600 12 601 PRT Aspergillus 12 Met Thr Glu Tyr Asp Tyr Ile Ile Val Gly Ala Gly Ile Gly Gly Leu 1 5 10 15 Val Leu Ala Asn Arg Leu Ser Ala Asp Ala Ser Val Asn Val Leu Leu 20 25 30 Ile Glu Ala Gly Ala Asn Arg Met Gly Asp Pro Arg Ile Asp Thr Pro 35 40 45 Gly Phe Leu Gly Met Leu Tyr Gly Asn Pro Asp Phe Asp Trp Asp Tyr 50 55 60 Met Ser Val Pro Gln Pro His Val Asn Asn Arg Gln Ile Ala Gln Pro 65 70 75 80 Arg Gly Arg Val Val Gly Gly Ser Ser Ala Leu Asn Phe Ser Val Val 85 90 95 Leu Tyr Pro Pro Ala Ser Asp Phe Glu Ala Trp Lys Ala Leu Gly Asn 100 105 110 Gln Gly Trp Gly Ala Glu Asp Met Ala Pro Tyr Leu Arg Lys Phe His 115 120 125 Thr Phe Ser Pro Pro Ser Lys Ser Thr Ala Asp Leu Leu Gly Val Asp 130 135 140 Ser Tyr Met Lys Ala Ser Ser Gln Gly Cys Asp Gly Pro Val Pro Val 145 150 155 160 Ser Leu Pro Asp Val Tyr Gly Pro Phe Asn Glu Ala Trp Asp Lys Thr 165 170 175 Phe Glu Lys Leu Gly Trp Arg Thr Asp Ala Asp Pro Ile Ala Gly Arg 180 185 190 Lys Leu Gly Ala Phe Thr Pro Pro Leu Thr Val Asp Ala Lys Thr Gly 195 200 205 Lys Arg Gly Tyr Ala Ala Ala Tyr Tyr Ser Pro Glu Val Ala Ala Arg 210 215 220 Pro Asn Leu Arg Leu Leu Ala Glu Thr Met Val Glu Arg Val Leu Leu 225 230 235 240 Thr Arg Gln Asp Gly Asp Val Leu Ala Thr Gly Val Leu Val Lys Asp 245 250 255 Lys Asp Gly Ala Arg Glu Ile His Ala Lys Lys Glu Val Ile Ile Cys 260 265 270 Ala Gly Ser Leu Asn Thr Pro Gln Ile Leu Glu Leu Ser Gly Ile Gly 275 280 285 Asn Ala Gly Leu Leu Gln Lys His Asp Ile Pro Val Val Ile Asp Asn 290 295 300 Pro Gly Val Gly Glu Asn Leu Gln Asp His Cys Ile Ser Cys Ile Ser 305 310 315 320 Phe Glu Ile Ala Asp Gly Gln Val Ser Gly Asp Ile Leu Arg Asp Pro 325 330 335 Asn Val Val Gln Ala Leu Val Lys Leu Tyr Glu Glu Thr Arg Gly Gly 340 345 350 Pro Leu Ala Gly Met Pro Ile Ser Val Ala Tyr Leu Pro Phe Val Asp 355 360 365 Gly Arg Gly Val Val Pro Arg Pro Glu Val Glu Glu Leu Leu Ala Lys 370 375 380 Tyr Leu Asp Ser Ala Ala Leu Pro Pro Asn Leu Gln Ala Gln Tyr Ala 385 390 395 400 His Leu Arg Lys Ala Ile Leu Asp Asn Asp Thr Pro Ser Ser Glu Tyr 405 410 415 Leu Phe Leu Pro Ala Gln Leu His Met Lys Pro Gly Ala Thr Ser Leu 420 425 430 Pro Asp Val Leu Ala Lys Pro Leu Pro Glu Asn Tyr Ile Ser Ile Met 435 440 445 Ile Leu His Asn His Pro Phe Ser Arg Gly Ser Val His Ile Ser Ser 450 455 460 Pro Lys Ala Glu Asp Lys Pro Ile Tyr Asp Pro Asn Phe Leu Ser His 465 470 475 480 Pro Leu Asp Leu Glu Ile Leu Ala Arg His Thr Gln Phe Leu Glu Thr 485 490 495 Ile Ala Ala Thr Glu Pro Phe Lys Ser Leu Leu Lys Glu Arg Arg Ile 500 505 510 Pro Glu Asn Ala Arg Asp Leu Gly Asp Leu Glu Arg Ala Lys Glu Leu 515 520 525 Val Lys Asp Arg Leu Phe Thr Cys Phe His Pro Ala Gly Thr Cys Ala 530 535 540 Met Leu Pro Arg Glu Met Gly Gly Val Val Asp Asp Gln Leu Arg Val 545 550 555 560 Tyr Gly Thr Arg Asn Leu Arg Val Val Asp Ala Ser Val Phe Pro Leu 565 570 575 Glu Pro Ala Gly Asn Ile Gln Ala Thr Val Tyr Ala Val Ala Glu Arg 580 585 590 Ala Ala Asp Leu Ile Ile Gly Ser Asn 595 600 13 1680 DNA Aspergillus 13 atgaagctcc aacgcctcct ctctatcacc ctcaccttta ccatcaccgc gccaacagcc 60 acagccacag cttcagcttc agctaaagca gatgcagaag cagaagcaga ctatctcgtc 120 accggtggcg gcacaaccgg cctcctcctc gccaaccgcc tctcttcaac acccacgacc 180 accgttttga tcctcgaccc cggcaacgac atccgcacga accccaatgt caccgatcca 240 acactctggc tccgcaacgc acacacagag gtcgactggg cctacccctc caccccccag 300 tcccacgccc tcaaccgcat cctctcctac accgccggcc gcatcctagg cggcacgagc 360 atgatcaacg ggatgacgta cctgcgcgcc gacaagcccg agatcgatgc gtgggaggca 420 ttaggtgcta aggggtggaa ttgggggagc ttgtggccgt attatttgcg cacggagaag 480 ttcagtccgc cgctgggatg gcaggtgggt gctggggcgg attatgtgcc tgatttacat 540 gggagaacgg ggagtgtgga tgtgtgtttc tcgatggagt tgtcacgggt agggttttgg 600 gagagggtga gggatgcgtg gagggttcta ggggtgaatt ggaatagaga tccgaatggg 660 gggtcggttg caggggtgtc ggtgtggccg cagacgattg attatcagga ggatgtgagg 720 tgtagttctg cgaaggcgtt ttattatcct gttgagggga gggagaatct gagggttgtg 780 aaggggaccg tcagaaggat tctttgggct gacacccggg gaggagagca tgtggcggcg 840 ggagtcgagt atctggatga gaacggacag atgcgaactg caacggcccg caaagaagtg 900 atcctgtcag ctggggcact gcggacaccc cccatcctgg aagcatcagg cgttggcgac 960 gcagacaggc tcagaggact tgggatagag acgcgaatcg atctccctgg cgtaggagag 020 aacctgcaag accaggcaaa cgtgcctctg ctatacacgg gaaacctcaa tatctcaggg 080 acctcgccgt acgccacgtt cctcatggca tcacagctct ttggcgagaa tctcgaagct 140 gtagctgcgt aagttccctc cgtctggctt gcacactggc tgacatgccg cagagagaca 200 ctctcctccg ttccgtcctg ggccgactcc ctcgcctcat cctcatccaa caacctcaac 260 agcagcgcga tagaacgcct cctcaccctc cagcacgccc tcatcttcaa atccaacgtc 320 actatagcag aaattctcac cagcgcgtcc ggaaccaccc tcctctctgc cttctggctc 1380 ctcctccctt tctcccgggg cagcgtgcac ctctcctcaa caaggcgaga agatataaac 1440 gcacccagca ttgacacaaa tttcttccag gtggactttg atctccagac cgagatggcc 1500 atagggagac tagcgcagtc attctgggaa caggggcccg tgaagagtct acatcccgtt 1560 ccgatgcccg gcagggcatt ggatgataat gcaacagaca cagaatggac agcgtttact 1620 aaagaaacct gtgagttgca tctggcagag aaaaatgaag aaaaggggca tactgattga 1680 14 1635 DNA Aspergillus CDS (1)...(1635) 14 atg aag ctc caa cgc ctc ctc tct atc acc ctc acc ttt acc atc acc 48 Met Lys Leu Gln Arg Leu Leu Ser Ile Thr Leu Thr Phe Thr Ile Thr 1 5 10 15 gcg cca aca gcc aca gcc aca gct tca gct tca gct aaa gca gat gca 96 Ala Pro Thr Ala Thr Ala Thr Ala Ser Ala Ser Ala Lys Ala Asp Ala 20 25 30 gaa gca gaa gca gac tat ctc gtc acc ggt ggc ggc aca acc ggc ctc 144 Glu Ala Glu Ala Asp Tyr Leu Val Thr Gly Gly Gly Thr Thr Gly Leu 35 40 45 ctc ctc gcc aac cgc ctc tct tca aca ccc acg acc acc gtt ttg atc 192 Leu Leu Ala Asn Arg Leu Ser Ser Thr Pro Thr Thr Thr Val Leu Ile 50 55 60 ctc gac ccc ggc aac gac atc cgc acg aac ccc aat gtc acc gat cca 240 Leu Asp Pro Gly Asn Asp Ile Arg Thr Asn Pro Asn Val Thr Asp Pro 65 70 75 80 aca ctc tgg ctc cgc aac gca cac aca gag gtc gac tgg gcc tac ccc 288 Thr Leu Trp Leu Arg Asn Ala His Thr Glu Val Asp Trp Ala Tyr Pro 85 90 95 tcc acc ccc cag tcc cac gcc ctc aac cgc atc ctc tcc tac acc gcc 336 Ser Thr Pro Gln Ser His Ala Leu Asn Arg Ile Leu Ser Tyr Thr Ala 100 105 110 ggc cgc atc cta ggc ggc acg agc atg atc aac ggg atg acg tac ctg 384 Gly Arg Ile Leu Gly Gly Thr Ser Met Ile Asn Gly Met Thr Tyr Leu 115 120 125 cgc gcc gac aag ccc gag atc gat gcg tgg gag gca tta ggt gct aag 432 Arg Ala Asp Lys Pro Glu Ile Asp Ala Trp Glu Ala Leu Gly Ala Lys 130 135 140 ggg tgg aat tgg ggg agc ttg tgg ccg tat tat ttg cgc acg gag aag 480 Gly Trp Asn Trp Gly Ser Leu Trp Pro Tyr Tyr Leu Arg Thr Glu Lys 145 150 155 160 ttc agt ccg ccg ctg gga tgg cag gtg ggt gct ggg gcg gat tat gtg 528 Phe Ser Pro Pro Leu Gly Trp Gln Val Gly Ala Gly Ala Asp Tyr Val 165 170 175 cct gat tta cat ggg aga acg ggg agt gtg gat gtg tgt ttc tcg atg 576 Pro Asp Leu His Gly Arg Thr Gly Ser Val Asp Val Cys Phe Ser Met 180 185 190 gag ttg tca cgg gta ggg ttt tgg gag agg gtg agg gat gcg tgg agg 624 Glu Leu Ser Arg Val Gly Phe Trp Glu Arg Val Arg Asp Ala Trp Arg 195 200 205 gtt cta ggg gtg aat tgg aat aga gat ccg aat ggg ggg tcg gtt gca 672 Val Leu Gly Val Asn Trp Asn Arg Asp Pro Asn Gly Gly Ser Val Ala 210 215 220 ggg gtg tcg gtg tgg ccg cag acg att gat tat cag gag gat gtg agg 720 Gly Val Ser Val Trp Pro Gln Thr Ile Asp Tyr Gln Glu Asp Val Arg 225 230 235 240 tgt agt tct gcg aag gcg ttt tat tat cct gtt gag ggg agg gag aat 768 Cys Ser Ser Ala Lys Ala Phe Tyr Tyr Pro Val Glu Gly Arg Glu Asn 245 250 255 ctg agg gtt gtg aag ggg acc gtc aga agg att ctt tgg gct gac acc 816 Leu Arg Val Val Lys Gly Thr Val Arg Arg Ile Leu Trp Ala Asp Thr 260 265 270 cgg gga gga gag cat gtg gcg gcg gga gtc gag tat ctg gat gag aac 864 Arg Gly Gly Glu His Val Ala Ala Gly Val Glu Tyr Leu Asp Glu Asn 275 280 285 gga cag atg cga act gca acg gcc cgc aaa gaa gtg atc ctg tca gct 912 Gly Gln Met Arg Thr Ala Thr Ala Arg Lys Glu Val Ile Leu Ser Ala 290 295 300 ggg gca ctg cgg aca ccc ccc atc ctg gaa gca tca ggc gtt ggc gac 960 Gly Ala Leu Arg Thr Pro Pro Ile Leu Glu Ala Ser Gly Val Gly Asp 305 310 315 320 gca gac agg ctc aga gga ctt ggg ata gag acg cga atc gat ctc cct 1008 Ala Asp Arg Leu Arg Gly Leu Gly Ile Glu Thr Arg Ile Asp Leu Pro 325 330 335 ggc gta gga gag aac ctg caa gac cag gca aac gtg cct ctg cta tac 1056 Gly Val Gly Glu Asn Leu Gln Asp Gln Ala Asn Val Pro Leu Leu Tyr 340 345 350 acg gga aac ctc aat atc tca ggg acc tcg ccg tac gcc acg ttc ctc 1104 Thr Gly Asn Leu Asn Ile Ser Gly Thr Ser Pro Tyr Ala Thr Phe Leu 355 360 365 atg gca tca cag ctc ttt ggc gag aat ctc gaa gct gta gct gca gag 1152 Met Ala Ser Gln Leu Phe Gly Glu Asn Leu Glu Ala Val Ala Ala Glu 370 375 380 aca ctc tcc tcc gtt ccg tcc tgg gcc gac tcc ctc gcc tca tcc tca 1200 Thr Leu Ser Ser Val Pro Ser Trp Ala Asp Ser Leu Ala Ser Ser Ser 385 390 395 400 tcc aac aac ctc aac agc agc gcg ata gaa cgc ctc ctc acc ctc cag 1248 Ser Asn Asn Leu Asn Ser Ser Ala Ile Glu Arg Leu Leu Thr Leu Gln 405 410 415 cac gcc ctc atc ttc aaa tcc aac gtc act ata gca gaa att ctc acc 1296 His Ala Leu Ile Phe Lys Ser Asn Val Thr Ile Ala Glu Ile Leu Thr 420 425 430 agc gcg tcc gga acc acc ctc ctc tct gcc ttc tgg ctc ctc ctc cct 1344 Ser Ala Ser Gly Thr Thr Leu Leu Ser Ala Phe Trp Leu Leu Leu Pro 435 440 445 ttc tcc cgg ggc agc gtg cac ctc tcc tca aca agg cga gaa gat ata 1392 Phe Ser Arg Gly Ser Val His Leu Ser Ser Thr Arg Arg Glu Asp Ile 450 455 460 aac gca ccc agc att gac aca aat ttc ttc cag gtg gac ttt gat ctc 1440 Asn Ala Pro Ser Ile Asp Thr Asn Phe Phe Gln Val Asp Phe Asp Leu 465 470 475 480 cag acc gag atg gcc ata ggg aga cta gcg cag tca ttc tgg gaa cag 1488 Gln Thr Glu Met Ala Ile Gly Arg Leu Ala Gln Ser Phe Trp Glu Gln 485 490 495 ggg ccc gtg aag agt cta cat ccc gtt ccg atg ccc ggc agg gca ttg 1536 Gly Pro Val Lys Ser Leu His Pro Val Pro Met Pro Gly Arg Ala Leu 500 505 510 gat gat aat gca aca gac aca gaa tgg aca gcg ttt act aaa gaa acc 1584 Asp Asp Asn Ala Thr Asp Thr Glu Trp Thr Ala Phe Thr Lys Glu Thr 515 520 525 tgt gag ttg cat ctg gca gag aaa aat gaa gaa aag ggg cat act gat 1632 Cys Glu Leu His Leu Ala Glu Lys Asn Glu Glu Lys Gly His Thr Asp 530 535 540 tga 1635 * 15 544 PRT Aspergillus 15 Met Lys Leu Gln Arg Leu Leu Ser Ile Thr Leu Thr Phe Thr Ile Thr 1 5 10 15 Ala Pro Thr Ala Thr Ala Thr Ala Ser Ala Ser Ala Lys Ala Asp Ala 20 25 30 Glu Ala Glu Ala Asp Tyr Leu Val Thr Gly Gly Gly Thr Thr Gly Leu 35 40 45 Leu Leu Ala Asn Arg Leu Ser Ser Thr Pro Thr Thr Thr Val Leu Ile 50 55 60 Leu Asp Pro Gly Asn Asp Ile Arg Thr Asn Pro Asn Val Thr Asp Pro 65 70 75 80 Thr Leu Trp Leu Arg Asn Ala His Thr Glu Val Asp Trp Ala Tyr Pro 85 90 95 Ser Thr Pro Gln Ser His Ala Leu Asn Arg Ile Leu Ser Tyr Thr Ala 100 105 110 Gly Arg Ile Leu Gly Gly Thr Ser Met Ile Asn Gly Met Thr Tyr Leu 115 120 125 Arg Ala Asp Lys Pro Glu Ile Asp Ala Trp Glu Ala Leu Gly Ala Lys 130 135 140 Gly Trp Asn Trp Gly Ser Leu Trp Pro Tyr Tyr Leu Arg Thr Glu Lys 145 150 155 160 Phe Ser Pro Pro Leu Gly Trp Gln Val Gly Ala Gly Ala Asp Tyr Val 165 170 175 Pro Asp Leu His Gly Arg Thr Gly Ser Val Asp Val Cys Phe Ser Met 180 185 190 Glu Leu Ser Arg Val Gly Phe Trp Glu Arg Val Arg Asp Ala Trp Arg 195 200 205 Val Leu Gly Val Asn Trp Asn Arg Asp Pro Asn Gly Gly Ser Val Ala 210 215 220 Gly Val Ser Val Trp Pro Gln Thr Ile Asp Tyr Gln Glu Asp Val Arg 225 230 235 240 Cys Ser Ser Ala Lys Ala Phe Tyr Tyr Pro Val Glu Gly Arg Glu Asn 245 250 255 Leu Arg Val Val Lys Gly Thr Val Arg Arg Ile Leu Trp Ala Asp Thr 260 265 270 Arg Gly Gly Glu His Val Ala Ala Gly Val Glu Tyr Leu Asp Glu Asn 275 280 285 Gly Gln Met Arg Thr Ala Thr Ala Arg Lys Glu Val Ile Leu Ser Ala 290 295 300 Gly Ala Leu Arg Thr Pro Pro Ile Leu Glu Ala Ser Gly Val Gly Asp 305 310 315 320 Ala Asp Arg Leu Arg Gly Leu Gly Ile Glu Thr Arg Ile Asp Leu Pro 325 330 335 Gly Val Gly Glu Asn Leu Gln Asp Gln Ala Asn Val Pro Leu Leu Tyr 340 345 350 Thr Gly Asn Leu Asn Ile Ser Gly Thr Ser Pro Tyr Ala Thr Phe Leu 355 360 365 Met Ala Ser Gln Leu Phe Gly Glu Asn Leu Glu Ala Val Ala Ala Glu 370 375 380 Thr Leu Ser Ser Val Pro Ser Trp Ala Asp Ser Leu Ala Ser Ser Ser 385 390 395 400 Ser Asn Asn Leu Asn Ser Ser Ala Ile Glu Arg Leu Leu Thr Leu Gln 405 410 415 His Ala Leu Ile Phe Lys Ser Asn Val Thr Ile Ala Glu Ile Leu Thr 420 425 430 Ser Ala Ser Gly Thr Thr Leu Leu Ser Ala Phe Trp Leu Leu Leu Pro 435 440 445 Phe Ser Arg Gly Ser Val His Leu Ser Ser Thr Arg Arg Glu Asp Ile 450 455 460 Asn Ala Pro Ser Ile Asp Thr Asn Phe Phe Gln Val Asp Phe Asp Leu 465 470 475 480 Gln Thr Glu Met Ala Ile Gly Arg Leu Ala Gln Ser Phe Trp Glu Gln 485 490 495 Gly Pro Val Lys Ser Leu His Pro Val Pro Met Pro Gly Arg Ala Leu 500 505 510 Asp Asp Asn Ala Thr Asp Thr Glu Trp Thr Ala Phe Thr Lys Glu Thr 515 520 525 Cys Glu Leu His Leu Ala Glu Lys Asn Glu Glu Lys Gly His Thr Asp 530 535 540 16 1943 DNA Aspergillus 16 atgattctca gtgcgttcat tctccttctc actctggtca ctgctctggc ccccgaatat 60 gacttcatca tcgtcggagg aggagtcagc ggccttgtcg tcgccaaccg tctctccgag 120 gaccccaacg tctccgttct catcatcgaa gccggtccat cagtccttga caacgagaat 180 gtgaccgatg tcgacgcgta ctcccgtgcg tttggtaccg aaatagactg gcagttcatc 240 agtgaatcac agctcttcgg cggagaacca cagatcctcc gggccggacg agcgctgggt 300 ggcgggagcg caatcaatgg tgaatcatcc ccatccggat atggatatga atatgcagaa 360 gagctaagac tgcgtttagg aatggcctac gtgcgtgctg aggacgtcca actggacgct 420 tggcagtcca tcggcaatga gcgctggaac tggacgagtc tgtttcctta ctatctcaag 480 agcgagaacc tgaccttgcc gacagccgtg cagacggatg caggcgcaac atacgatgcc 540 tttgcgcatg gcacccgcgg tcccctcaag gttgctttcc cacgtatgca gagtggtgat 600 aatgatctga cacctgcggt caaccagacg cttcaggctg cggggattcc gtggaacgta 660 gatgtgaatg ctgggcgcat gcgtggattt agtatttacc cctggaccat cgatgaggag 720 gcgtatattc ggtatgatgc cgctcgggct tatttttggc cgtttcagtc gcgatcgaac 780 ctgcatgcct ggttgaacac gagggtgaat cggattgttt ggagagacgt gcctggtgga 840 gagaacaccc gtgcagctgg cgtggaggtt acttcacagc atggcactgt aagtgttgtg 900 atgtcgagaa gagaggtgat tctctcggct ggagcgctca agtcgcccgc cattcttgag 960 ctttccggga tcgggaatcc acggtgagtt gcttctcggt cttatatccg cgataaacgg 1020 gcttgagctg aggcactgaa actcccttat agcatcctca atcaacacaa catccccgtt 1080 cacgtctcac tcccaggcgt cggagaaaac ttacaggatc agatgaacac tctcatgaca 1140 gcgtcgaccc attcacccat caccggcggc agaaccgtca ctttcgcatc ggccacggac 1200 atcttcagtc aggatatctc ctccctcgcc aacctcacac ataccaagct cccctcgtac 1260 gctgccctcg tcgcaaacat gagcaacgga gccatgcaac ccgaacacct gcgggctgta 1320 ttccaagtgc aacacgacct tatcttcaag aacaacattc ccattgcaga aataatcttc 1380 aagcccggcg gcgagaaaac cgtcaacgcc gggttctggg gcctcctccc ctttgcacgc 1440 gggaacgtgc acatccgctc ttctgatccg gcagcccagc ccgcgatcag tcccaattac 1500 ggcctgttgg actgggatat ccagttgcag gttgcaattg ccaagttcat ccggcggatg 1560 tttcgctctg cgccgcttga ggggatgatt gaggaggaat cgaggcctgg tctgtcggcg 1620 gtgcctgggg atgccgcgga tgaggtgtgg gggaactggt tggaagataa ctgtacgtgg 1680 ggtaattttc tctttttcct aggagatgtc tctaactcag tgctgtagat gcgtccaact 1740 tccatgccat cggcacagcg gccatgatgc cccgttctct aggtggagtc gtcaacgatc 1800 ggctgcaggt gtacggcacg gcgaatgttc gcgttgtcga tgcgtctatt catccgcttc 1860 agctttgcgg tcatccgatg gctaacctgt acgctattgc agagcgcaca gcggatttga 1920 tcaaggagga ttggacgggc taa 1943 17 1758 DNA Aspergillus CDS (1)...(1758) 17 atg att ctc agt gcg ttc att ctc ctt ctc act ctg gtc act gct ctg 48 Met Ile Leu Ser Ala Phe Ile Leu Leu Leu Thr Leu Val Thr Ala Leu 1 5 10 15 gcc ccc gaa tat gac ttc atc atc gtc gga gga gga gtc agc ggc ctt 96 Ala Pro Glu Tyr Asp Phe Ile Ile Val Gly Gly Gly Val Ser Gly Leu 20 25 30 gtc gtc gcc aac cgt ctc tcc gag gac ccc aac gtc tcc gtt ctc atc 144 Val Val Ala Asn Arg Leu Ser Glu Asp Pro Asn Val Ser Val Leu Ile 35 40 45 atc gaa gcc ggt cca tca gtc ctt gac aac gag aat gtg acc gat gtc 192 Ile Glu Ala Gly Pro Ser Val Leu Asp Asn Glu Asn Val Thr Asp Val 50 55 60 gac gcg tac tcc cgt gcg ttt ggt acc gaa ata gac tgg cag ttc atc 240 Asp Ala Tyr Ser Arg Ala Phe Gly Thr Glu Ile Asp Trp Gln Phe Ile 65 70 75 80 agt gaa tca cag ctc ttc ggc gga gaa cca cag atc ctc cgg gcc gga 288 Ser Glu Ser Gln Leu Phe Gly Gly Glu Pro Gln Ile Leu Arg Ala Gly 85 90 95 cga gcg ctg ggt ggc ggg agc gca atc aat gga atg gcc tac gtg cgt 336 Arg Ala Leu Gly Gly Gly Ser Ala Ile Asn Gly Met Ala Tyr Val Arg 100 105 110 gct gag gac gtc caa ctg gac gct tgg cag tcc atc ggc aat gag cgc 384 Ala Glu Asp Val Gln Leu Asp Ala Trp Gln Ser Ile Gly Asn Glu Arg 115 120 125 tgg aac tgg acg agt ctg ttt cct tac tat ctc aag agc gag aac ctg 432 Trp Asn Trp Thr Ser Leu Phe Pro Tyr Tyr Leu Lys Ser Glu Asn Leu 130 135 140 acc ttg ccg aca gcc gtg cag acg gat gca ggc gca aca tac gat gcc 480 Thr Leu Pro Thr Ala Val Gln Thr Asp Ala Gly Ala Thr Tyr Asp Ala 145 150 155 160 ttt gcg cat ggc acc cgc ggt ccc ctc aag gtt gct ttc cca cgt atg 528 Phe Ala His Gly Thr Arg Gly Pro Leu Lys Val Ala Phe Pro Arg Met 165 170 175 cag agt ggt gat aat gat ctg aca cct gcg gtc aac cag acg ctt cag 576 Gln Ser Gly Asp Asn Asp Leu Thr Pro Ala Val Asn Gln Thr Leu Gln 180 185 190 gct gcg ggg att ccg tgg aac gta gat gtg aat gct ggg cgc atg cgt 624 Ala Ala Gly Ile Pro Trp Asn Val Asp Val Asn Ala Gly Arg Met Arg 195 200 205 gga ttt agt att tac ccc tgg acc atc gat gag gag gcg tat att cgg 672 Gly Phe Ser Ile Tyr Pro Trp Thr Ile Asp Glu Glu Ala Tyr Ile Arg 210 215 220 tat gat gcc gct cgg gct tat ttt tgg ccg ttt cag tcg cga tcg aac 720 Tyr Asp Ala Ala Arg Ala Tyr Phe Trp Pro Phe Gln Ser Arg Ser Asn 225 230 235 240 ctg cat gcc tgg ttg aac acg agg gtg aat cgg att gtt tgg aga gac 768 Leu His Ala Trp Leu Asn Thr Arg Val Asn Arg Ile Val Trp Arg Asp 245 250 255 gtg cct ggt gga gag aac acc cgt gca gct ggc gtg gag gtt act tca 816 Val Pro Gly Gly Glu Asn Thr Arg Ala Ala Gly Val Glu Val Thr Ser 260 265 270 cag cat ggc act gta agt gtt gtg atg tcg aga aga gag gtg att ctc 864 Gln His Gly Thr Val Ser Val Val Met Ser Arg Arg Glu Val Ile Leu 275 280 285 tcg gct gga gcg ctc aag tcg ccc gcc att ctt gag ctt tcc ggg atc 912 Ser Ala Gly Ala Leu Lys Ser Pro Ala Ile Leu Glu Leu Ser Gly Ile 290 295 300 ggg aat cca cgc atc ctc aat caa cac aac atc ccc gtt cac gtc tca 960 Gly Asn Pro Arg Ile Leu Asn Gln His Asn Ile Pro Val His Val Ser 305 310 315 320 ctc cca ggc gtc gga gaa aac tta cag gat cag atg aac act ctc atg 1008 Leu Pro Gly Val Gly Glu Asn Leu Gln Asp Gln Met Asn Thr Leu Met 325 330 335 aca gcg tcg acc cat tca ccc atc acc ggc ggc aga acc gtc act ttc 1056 Thr Ala Ser Thr His Ser Pro Ile Thr Gly Gly Arg Thr Val Thr Phe 340 345 350 gca tcg gcc acg gac atc ttc agt cag gat atc tcc tcc ctc gcc aac 1104 Ala Ser Ala Thr Asp Ile Phe Ser Gln Asp Ile Ser Ser Leu Ala Asn 355 360 365 ctc aca cat acc aag ctc ccc tcg tac gct gcc ctc gtc gca aac atg 1152 Leu Thr His Thr Lys Leu Pro Ser Tyr Ala Ala Leu Val Ala Asn Met 370 375 380 agc aac gga gcc atg caa ccc gaa cac ctg cgg gct gta ttc caa gtg 1200 Ser Asn Gly Ala Met Gln Pro Glu His Leu Arg Ala Val Phe Gln Val 385 390 395 400 caa cac gac ctt atc ttc aag aac aac att ccc att gca gaa ata atc 1248 Gln His Asp Leu Ile Phe Lys Asn Asn Ile Pro Ile Ala Glu Ile Ile 405 410 415 ttc aag ccc ggc ggc gag aaa acc gtc aac gcc ggg ttc tgg ggc ctc 1296 Phe Lys Pro Gly Gly Glu Lys Thr Val Asn Ala Gly Phe Trp Gly Leu 420 425 430 ctc ccc ttt gca cgc ggg aac gtg cac atc cgc tct tct gat ccg gca 1344 Leu Pro Phe Ala Arg Gly Asn Val His Ile Arg Ser Ser Asp Pro Ala 435 440 445 gcc cag ccc gcg atc agt ccc aat tac ggc ctg ttg gac tgg gat atc 1392 Ala Gln Pro Ala Ile Ser Pro Asn Tyr Gly Leu Leu Asp Trp Asp Ile 450 455 460 cag ttg cag gtt gca att gcc aag ttc atc cgg cgg atg ttt cgc tct 1440 Gln Leu Gln Val Ala Ile Ala Lys Phe Ile Arg Arg Met Phe Arg Ser 465 470 475 480 gcg ccg ctt gag ggg atg att gag gag gaa tcg agg cct ggt ctg tcg 1488 Ala Pro Leu Glu Gly Met Ile Glu Glu Glu Ser Arg Pro Gly Leu Ser 485 490 495 gcg gtg cct ggg gat gcc gcg gat gag gtg tgg ggg aac tgg ttg gaa 1536 Ala Val Pro Gly Asp Ala Ala Asp Glu Val Trp Gly Asn Trp Leu Glu 500 505 510 gat aac tat gcg tcc aac ttc cat gcc atc ggc aca gcg gcc atg atg 1584 Asp Asn Tyr Ala Ser Asn Phe His Ala Ile Gly Thr Ala Ala Met Met 515 520 525 ccc cgt tct cta ggt gga gtc gtc aac gat cgg ctg cag gtg tac ggc 1632 Pro Arg Ser Leu Gly Gly Val Val Asn Asp Arg Leu Gln Val Tyr Gly 530 535 540 acg gcg aat gtt cgc gtt gtc gat gcg tct att cat ccg ctt cag ctt 1680 Thr Ala Asn Val Arg Val Val Asp Ala Ser Ile His Pro Leu Gln Leu 545 550 555 560 tgc ggt cat ccg atg gct aac ctg tac gct att gca gag cgc aca gcg 1728 Cys Gly His Pro Met Ala Asn Leu Tyr Ala Ile Ala Glu Arg Thr Ala 565 570 575 gat ttg atc aag gag gat tgg acg ggc taa 1758 Asp Leu Ile Lys Glu Asp Trp Thr Gly * 580 585 18 585 PRT Aspergillus 18 Met Ile Leu Ser Ala Phe Ile Leu Leu Leu Thr Leu Val Thr Ala Leu 1 5 10 15 Ala Pro Glu Tyr Asp Phe Ile Ile Val Gly Gly Gly Val Ser Gly Leu 20 25 30 Val Val Ala Asn Arg Leu Ser Glu Asp Pro Asn Val Ser Val Leu Ile 35 40 45 Ile Glu Ala Gly Pro Ser Val Leu Asp Asn Glu Asn Val Thr Asp Val 50 55 60 Asp Ala Tyr Ser Arg Ala Phe Gly Thr Glu Ile Asp Trp Gln Phe Ile 65 70 75 80 Ser Glu Ser Gln Leu Phe Gly Gly Glu Pro Gln Ile Leu Arg Ala Gly 85 90 95 Arg Ala Leu Gly Gly Gly Ser Ala Ile Asn Gly Met Ala Tyr Val Arg 100 105 110 Ala Glu Asp Val Gln Leu Asp Ala Trp Gln Ser Ile Gly Asn Glu Arg 115 120 125 Trp Asn Trp Thr Ser Leu Phe Pro Tyr Tyr Leu Lys Ser Glu Asn Leu 130 135 140 Thr Leu Pro Thr Ala Val Gln Thr Asp Ala Gly Ala Thr Tyr Asp Ala 145 150 155 160 Phe Ala His Gly Thr Arg Gly Pro Leu Lys Val Ala Phe Pro Arg Met 165 170 175 Gln Ser Gly Asp Asn Asp Leu Thr Pro Ala Val Asn Gln Thr Leu Gln 180 185 190 Ala Ala Gly Ile Pro Trp Asn Val Asp Val Asn Ala Gly Arg Met Arg 195 200 205 Gly Phe Ser Ile Tyr Pro Trp Thr Ile Asp Glu Glu Ala Tyr Ile Arg 210 215 220 Tyr Asp Ala Ala Arg Ala Tyr Phe Trp Pro Phe Gln Ser Arg Ser Asn 225 230 235 240 Leu His Ala Trp Leu Asn Thr Arg Val Asn Arg Ile Val Trp Arg Asp 245 250 255 Val Pro Gly Gly Glu Asn Thr Arg Ala Ala Gly Val Glu Val Thr Ser 260 265 270 Gln His Gly Thr Val Ser Val Val Met Ser Arg Arg Glu Val Ile Leu 275 280 285 Ser Ala Gly Ala Leu Lys Ser Pro Ala Ile Leu Glu Leu Ser Gly Ile 290 295 300 Gly Asn Pro Arg Ile Leu Asn Gln His Asn Ile Pro Val His Val Ser 305 310 315 320 Leu Pro Gly Val Gly Glu Asn Leu Gln Asp Gln Met Asn Thr Leu Met 325 330 335 Thr Ala Ser Thr His Ser Pro Ile Thr Gly Gly Arg Thr Val Thr Phe 340 345 350 Ala Ser Ala Thr Asp Ile Phe Ser Gln Asp Ile Ser Ser Leu Ala Asn 355 360 365 Leu Thr His Thr Lys Leu Pro Ser Tyr Ala Ala Leu Val Ala Asn Met 370 375 380 Ser Asn Gly Ala Met Gln Pro Glu His Leu Arg Ala Val Phe Gln Val 385 390 395 400 Gln His Asp Leu Ile Phe Lys Asn Asn Ile Pro Ile Ala Glu Ile Ile 405 410 415 Phe Lys Pro Gly Gly Glu Lys Thr Val Asn Ala Gly Phe Trp Gly Leu 420 425 430 Leu Pro Phe Ala Arg Gly Asn Val His Ile Arg Ser Ser Asp Pro Ala 435 440 445 Ala Gln Pro Ala Ile Ser Pro Asn Tyr Gly Leu Leu Asp Trp Asp Ile 450 455 460 Gln Leu Gln Val Ala Ile Ala Lys Phe Ile Arg Arg Met Phe Arg Ser 465 470 475 480 Ala Pro Leu Glu Gly Met Ile Glu Glu Glu Ser Arg Pro Gly Leu Ser 485 490 495 Ala Val Pro Gly Asp Ala Ala Asp Glu Val Trp Gly Asn Trp Leu Glu 500 505 510 Asp Asn Tyr Ala Ser Asn Phe His Ala Ile Gly Thr Ala Ala Met Met 515 520 525 Pro Arg Ser Leu Gly Gly Val Val Asn Asp Arg Leu Gln Val Tyr Gly 530 535 540 Thr Ala Asn Val Arg Val Val Asp Ala Ser Ile His Pro Leu Gln Leu 545 550 555 560 Cys Gly His Pro Met Ala Asn Leu Tyr Ala Ile Ala Glu Arg Thr Ala 565 570 575 Asp Leu Ile Lys Glu Asp Trp Thr Gly 580 585 19 2353 DNA Aspergillus 19 atgcagcaag aaggggtctc aggtggttcg tctctttcgg tcttggagtg tgaccgctca 60 gcttctcgtt tcaattttcc ttatttccct accatcatca tcatcattat catcatcatc 120 atcactgtga tctattcaag gcagtcatcg ataagagcat gtgaaagttg tgcatgcgag 180 gcagtctcca tccgccttga tgaaatgaaa gatgaaacgc cgcgaatgac cgagatgaca 240 aggaagccgt tcctgacgat cgccataggc gtcttgacca ctgtcagcgc tctctcggac 300 cccgctcaga ttgtgattcc agcaacaata acaccccaga cgacggaccc cttggtgtca 360 tggttagcgc aagaaacttc atacgccctc gatggtgtgt taaacaatgt cggaccgaac 420 ggggctaagg caactggcgc tagctctggc atcatcatcg ctagtcctag ccaaagcaat 480 ccggactgtg agtaattact tcctccgtac catttcactg caactgactc ggctgacctg 540 tggttgagac tactatacct ggactcgaga cgccgctctc accgtcaaat acctcgttgg 600 ttcttttgcc gccgatcacg atcctgcaat ccaaaggatc atagaggatt acgtagaatc 660 ccaggcgcac ttgcagactg tctccaaccc ttccggaaat ctatcaagcg gaggcttggg 720 ggaacctaag ttgagggtgg atggatcggc attccatggc tcctgggggc gtccacagag 780 tgatgggcct gcgctgagag caacaacact gatatcctac gcaaacttga tgattgtatg 840 tttttgctct tttcaataaa gattgagctt cctaacttcg tgtactctaa taggataatg 900 gttatttctc taccgttgag tcaagcatct ggccaatcat tcagaatgac ctttcctatc 960 taacggagtt ttggaactct tctacttttg gtacgtttgt gtgtttctca tacgggagga 1020 tcatccagtg accagatccg gtagatcttt gggaggaagt tcgcggttcc tcatttttca 1080 ccacggcagt ccagcatcaa gccctcagaa aaggtgcagc ccttgcccag aggcttggta 1140 aaacctgttc aaactgccag tcacaggcac cgcaggttct ctgtttcctg cagacttact 1200 ggactggctc gtccatactg gccaatctgt atagtgatcg gtccgggaaa gatgccaatt 1260 caatactagg catcatccat acttttgacc ccaatgcggg ctgcgacgga cagacgttcc 1320 aaccgtgttc tgatcgggcg cttgcaagcc acaaggaagt cgtagactcc ttccgctcgc 1380 tgtacccgat caatgcagac attccccagg gccaagctgt agccgtgggt cggtacccag 1440 aggatgtcta tcaaggtgga cacccttggt atctgtgcac tttggcagca gctgagcagc 1500 tatacgatgc actttatcag tgggagagat tggggtccct cgccgttaca aatataagcc 1560 tcgcgttctt ccaggacttg gtcccatcag ctacagttgg gacatacgcg aaggacacca 1620 tcacatttgc ctctatatct gcagctgttc gagattacgc agatcgattt ctccgaatcg 1680 tggtaggtgt tactctctaa cttttttttt ggccagaacc gtgtcaagca ctaacatgac 1740 ctcacagcag aaatacacac ccccgaatgg cgccctcgca gagcaattct cgcgctatga 1800 cggctccccc ctctcagcgc aagacctcac ttggtcctac acatcctttc tcactgcagt 1860 tcaagcccga agacatgctc ttaatccttc cgcatcacac atccaacctc tcctctcaaa 1920 cgcgaccacc gccactgccc tcccccaagt ctgcacccct tcctccgcac gagggcccta 1980 ccagcccgtt aaacgaatca agtggcccag accagagtgt ctctcccctc ggagtaccgt 2040 cgccgttcgg ttcaatgtcc tggcgaccac cgttattggc gaggacatct tcctcgtcgg 2100 gtccatcccc gcgctgggcg aatgggatgc gcggcatcag gctttgaagt tggaagcgaa 2160 tgagtactcg agcatcacgc ccttgtggta caggaccgtg atgttggatg ccggggagga 2220 gtttgaatat aaattcattc ggaaaagggt gggtgacggt aaggtaatct gggaagaagg 2280 ccagaatcga gcatttgtgg tgccgagaga gtgtggccct tccaatgcga caatcaatgc 2340 cgtctggaga tga 2353 20 2115 DNA Aspergillus CDS (1)...(2115) 20 atg cag caa gaa ggg gtc tca ggt ggt tcg tct ctt tcg gtc ttg gag 48 Met Gln Gln Glu Gly Val Ser Gly Gly Ser Ser Leu Ser Val Leu Glu 1 5 10 15 tgt gac cgc tca gct tct cgt ttc aat ttt cct tat ttc cct acc atc 96 Cys Asp Arg Ser Ala Ser Arg Phe Asn Phe Pro Tyr Phe Pro Thr Ile 20 25 30 atc atc atc att atc atc atc atc atc act gtg atc tat tca agg cag 144 Ile Ile Ile Ile Ile Ile Ile Ile Ile Thr Val Ile Tyr Ser Arg Gln 35 40 45 tca tcg ata aga gca tgt gaa agt tgt gca tgc gag gca gtc tcc atc 192 Ser Ser Ile Arg Ala Cys Glu Ser Cys Ala Cys Glu Ala Val Ser Ile 50 55 60 cgc ctt gat gaa atg aaa gat gaa acg ccg cga atg acc gag atg aca 240 Arg Leu Asp Glu Met Lys Asp Glu Thr Pro Arg Met Thr Glu Met Thr 65 70 75 80 agg aag ccg ttc ctg acg atc gcc ata ggc gtc ttg acc act gtc agc 288 Arg Lys Pro Phe Leu Thr Ile Ala Ile Gly Val Leu Thr Thr Val Ser 85 90 95 gct ctc tcg gac ccc gct cag att gtg att cca gca aca ata aca ccc 336 Ala Leu Ser Asp Pro Ala Gln Ile Val Ile Pro Ala Thr Ile Thr Pro 100 105 110 cag acg acg gac ccc ttg gtg tca tgg tta gcg caa gaa act tca tac 384 Gln Thr Thr Asp Pro Leu Val Ser Trp Leu Ala Gln Glu Thr Ser Tyr 115 120 125 gcc ctc gat ggt gtg tta aac aat gtc gga ccg aac ggg gct aag gca 432 Ala Leu Asp Gly Val Leu Asn Asn Val Gly Pro Asn Gly Ala Lys Ala 130 135 140 act ggc gct agc tct ggc atc atc atc gct agt cct agc caa agc aat 480 Thr Gly Ala Ser Ser Gly Ile Ile Ile Ala Ser Pro Ser Gln Ser Asn 145 150 155 160 ccg gac tac tac tat acc tgg act cga gac gcc gct ctc acc gtc aaa 528 Pro Asp Tyr Tyr Tyr Thr Trp Thr Arg Asp Ala Ala Leu Thr Val Lys 165 170 175 tac ctc gtt ggt tct ttt gcc gcc gat cac gat cct gca atc caa agg 576 Tyr Leu Val Gly Ser Phe Ala Ala Asp His Asp Pro Ala Ile Gln Arg 180 185 190 atc ata gag gat tac gta gaa tcc cag gcg cac ttg cag act gtc tcc 624 Ile Ile Glu Asp Tyr Val Glu Ser Gln Ala His Leu Gln Thr Val Ser 195 200 205 aac cct tcc gga aat cta tca agc gga ggc ttg ggg gaa cct aag ttg 672 Asn Pro Ser Gly Asn Leu Ser Ser Gly Gly Leu Gly Glu Pro Lys Leu 210 215 220 agg gtg gat gga tcg gca ttc cat ggc tcc tgg ggg cgt cca cag agt 720 Arg Val Asp Gly Ser Ala Phe His Gly Ser Trp Gly Arg Pro Gln Ser 225 230 235 240 gat ggg cct gcg ctg aga gca aca aca ctg ata tcc tac gca aac ttg 768 Asp Gly Pro Ala Leu Arg Ala Thr Thr Leu Ile Ser Tyr Ala Asn Leu 245 250 255 atg att gat aat ggt tat ttc tct acc gtt gag tca agc atc tgg cca 816 Met Ile Asp Asn Gly Tyr Phe Ser Thr Val Glu Ser Ser Ile Trp Pro 260 265 270 atc att cag aat gac ctt tcc tat cta acg gag ttt tgg aac tct tct 864 Ile Ile Gln Asn Asp Leu Ser Tyr Leu Thr Glu Phe Trp Asn Ser Ser 275 280 285 act ttt gat ctt tgg gag gaa gtt cgc ggt tcc tca ttt ttc acc acg 912 Thr Phe Asp Leu Trp Glu Glu Val Arg Gly Ser Ser Phe Phe Thr Thr 290 295 300 gca gtc cag cat caa gcc ctc aga aaa ggt gca gcc ctt gcc cag agg 960 Ala Val Gln His Gln Ala Leu Arg Lys Gly Ala Ala Leu Ala Gln Arg 305 310 315 320 ctt ggt aaa acc tgt tca aac tgc cag tca cag gca ccg cag gtt ctc 1008 Leu Gly Lys Thr Cys Ser Asn Cys Gln Ser Gln Ala Pro Gln Val Leu 325 330 335 tgt ttc ctg cag act tac tgg act ggc tcg tcc ata ctg gcc aat ctg 1056 Cys Phe Leu Gln Thr Tyr Trp Thr Gly Ser Ser Ile Leu Ala Asn Leu 340 345 350 tat agt gat cgg tcc ggg aaa gat gcc aat tca ata cta ggc atc atc 1104 Tyr Ser Asp Arg Ser Gly Lys Asp Ala Asn Ser Ile Leu Gly Ile Ile 355 360 365 cat act ttt gac ccc aat gcg ggc tgc gac gga cag acg ttc caa ccg 1152 His Thr Phe Asp Pro Asn Ala Gly Cys Asp Gly Gln Thr Phe Gln Pro 370 375 380 tgt tct gat cgg gcg ctt gca agc cac aag gaa gtc gta gac tcc ttc 1200 Cys Ser Asp Arg Ala Leu Ala Ser His Lys Glu Val Val Asp Ser Phe 385 390 395 400 cgc tcg ctg tac ccg atc aat gca gac att ccc cag ggc caa gct gta 1248 Arg Ser Leu Tyr Pro Ile Asn Ala Asp Ile Pro Gln Gly Gln Ala Val 405 410 415 gcc gtg ggt cgg tac cca gag gat gtc tat caa ggt gga cac cct tgg 1296 Ala Val Gly Arg Tyr Pro Glu Asp Val Tyr Gln Gly Gly His Pro Trp 420 425 430 tat ctg tgc act ttg gca gca gct gag cag cta tac gat gca ctt tat 1344 Tyr Leu Cys Thr Leu Ala Ala Ala Glu Gln Leu Tyr Asp Ala Leu Tyr 435 440 445 cag tgg gag aga ttg ggg tcc ctc gcc gtt aca aat ata agc ctc gcg 1392 Gln Trp Glu Arg Leu Gly Ser Leu Ala Val Thr Asn Ile Ser Leu Ala 450 455 460 ttc ttc cag gac ttg gtc cca tca gct aca gtt ggg aca tac gcg aag 1440 Phe Phe Gln Asp Leu Val Pro Ser Ala Thr Val Gly Thr Tyr Ala Lys 465 470 475 480 gac acc atc aca ttt gcc tct ata tct gca gct gtt cga gat tac gca 1488 Asp Thr Ile Thr Phe Ala Ser Ile Ser Ala Ala Val Arg Asp Tyr Ala 485 490 495 gat cga ttt ctc cga atc gtg cag aaa tac aca ccc ccg aat ggc gcc 1536 Asp Arg Phe Leu Arg Ile Val Gln Lys Tyr Thr Pro Pro Asn Gly Ala 500 505 510 ctc gca gag caa ttc tcg cgc tat gac ggc tcc ccc ctc tca gcg caa 1584 Leu Ala Glu Gln Phe Ser Arg Tyr Asp Gly Ser Pro Leu Ser Ala Gln 515 520 525 gac ctc act tgg tcc tac aca tcc ttt ctc act gca gtt caa gcc cga 1632 Asp Leu Thr Trp Ser Tyr Thr Ser Phe Leu Thr Ala Val Gln Ala Arg 530 535 540 aga cat gct ctt aat cct tcc gca tca cac atc caa cct ctc ctc tca 1680 Arg His Ala Leu Asn Pro Ser Ala Ser His Ile Gln Pro Leu Leu Ser 545 550 555 560 aac gcg acc acc gcc act gcc ctc ccc caa gtc tgc acc cct tcc tcc 1728 Asn Ala Thr Thr Ala Thr Ala Leu Pro Gln Val Cys Thr Pro Ser Ser 565 570 575 gca cga ggg ccc tac cag ccc gtt aaa cga atc aag tgg ccc aga cca 1776 Ala Arg Gly Pro Tyr Gln Pro Val Lys Arg Ile Lys Trp Pro Arg Pro 580 585 590 gag tgt ctc tcc cct cgg agt acc gtc gcc gtt cgg ttc aat gtc ctg 1824 Glu Cys Leu Ser Pro Arg Ser Thr Val Ala Val Arg Phe Asn Val Leu 595 600 605 gcg acc acc gtt att ggc gag gac atc ttc ctc gtc ggg tcc atc ccc 1872 Ala Thr Thr Val Ile Gly Glu Asp Ile Phe Leu Val Gly Ser Ile Pro 610 615 620 gcg ctg ggc gaa tgg gat gcg cgg cat cag gct ttg aag ttg gaa gcg 1920 Ala Leu Gly Glu Trp Asp Ala Arg His Gln Ala Leu Lys Leu Glu Ala 625 630 635 640 aat gag tac tcg agc atc acg ccc ttg tgg tac agg acc gtg atg ttg 1968 Asn Glu Tyr Ser Ser Ile Thr Pro Leu Trp Tyr Arg Thr Val Met Leu 645 650 655 gat gcc ggg gag gag ttt gaa tat aaa ttc att cgg aaa agg gtg ggt 2016 Asp Ala Gly Glu Glu Phe Glu Tyr Lys Phe Ile Arg Lys Arg Val Gly 660 665 670 gac ggt aag gta atc tgg gaa gaa ggc cag aat cga gca ttt gtg gtg 2064 Asp Gly Lys Val Ile Trp Glu Glu Gly Gln Asn Arg Ala Phe Val Val 675 680 685 ccg aga gag tgt ggc cct tcc aat gcg aca atc aat gcc gtc tgg aga 2112 Pro Arg Glu Cys Gly Pro Ser Asn Ala Thr Ile Asn Ala Val Trp Arg 690 695 700 tga 2115 * 21 704 PRT Aspergillus 21 Met Gln Gln Glu Gly Val Ser Gly Gly Ser Ser Leu Ser Val Leu Glu 1 5 10 15 Cys Asp Arg Ser Ala Ser Arg Phe Asn Phe Pro Tyr Phe Pro Thr Ile 20 25 30 Ile Ile Ile Ile Ile Ile Ile Ile Ile Thr Val Ile Tyr Ser Arg Gln 35 40 45 Ser Ser Ile Arg Ala Cys Glu Ser Cys Ala Cys Glu Ala Val Ser Ile 50 55 60 Arg Leu Asp Glu Met Lys Asp Glu Thr Pro Arg Met Thr Glu Met Thr 65 70 75 80 Arg Lys Pro Phe Leu Thr Ile Ala Ile Gly Val Leu Thr Thr Val Ser 85 90 95 Ala Leu Ser Asp Pro Ala Gln Ile Val Ile Pro Ala Thr Ile Thr Pro 100 105 110 Gln Thr Thr Asp Pro Leu Val Ser Trp Leu Ala Gln Glu Thr Ser Tyr 115 120 125 Ala Leu Asp Gly Val Leu Asn Asn Val Gly Pro Asn Gly Ala Lys Ala 130 135 140 Thr Gly Ala Ser Ser Gly Ile Ile Ile Ala Ser Pro Ser Gln Ser Asn 145 150 155 160 Pro Asp Tyr Tyr Tyr Thr Trp Thr Arg Asp Ala Ala Leu Thr Val Lys 165 170 175 Tyr Leu Val Gly Ser Phe Ala Ala Asp His Asp Pro Ala Ile Gln Arg 180 185 190 Ile Ile Glu Asp Tyr Val Glu Ser Gln Ala His Leu Gln Thr Val Ser 195 200 205 Asn Pro Ser Gly Asn Leu Ser Ser Gly Gly Leu Gly Glu Pro Lys Leu 210 215 220 Arg Val Asp Gly Ser Ala Phe His Gly Ser Trp Gly Arg Pro Gln Ser 225 230 235 240 Asp Gly Pro Ala Leu Arg Ala Thr Thr Leu Ile Ser Tyr Ala Asn Leu 245 250 255 Met Ile Asp Asn Gly Tyr Phe Ser Thr Val Glu Ser Ser Ile Trp Pro 260 265 270 Ile Ile Gln Asn Asp Leu Ser Tyr Leu Thr Glu Phe Trp Asn Ser Ser 275 280 285 Thr Phe Asp Leu Trp Glu Glu Val Arg Gly Ser Ser Phe Phe Thr Thr 290 295 300 Ala Val Gln His Gln Ala Leu Arg Lys Gly Ala Ala Leu Ala Gln Arg 305 310 315 320 Leu Gly Lys Thr Cys Ser Asn Cys Gln Ser Gln Ala Pro Gln Val Leu 325 330 335 Cys Phe Leu Gln Thr Tyr Trp Thr Gly Ser Ser Ile Leu Ala Asn Leu 340 345 350 Tyr Ser Asp Arg Ser Gly Lys Asp Ala Asn Ser Ile Leu Gly Ile Ile 355 360 365 His Thr Phe Asp Pro Asn Ala Gly Cys Asp Gly Gln Thr Phe Gln Pro 370 375 380 Cys Ser Asp Arg Ala Leu Ala Ser His Lys Glu Val Val Asp Ser Phe 385 390 395 400 Arg Ser Leu Tyr Pro Ile Asn Ala Asp Ile Pro Gln Gly Gln Ala Val 405 410 415 Ala Val Gly Arg Tyr Pro Glu Asp Val Tyr Gln Gly Gly His Pro Trp 420 425 430 Tyr Leu Cys Thr Leu Ala Ala Ala Glu Gln Leu Tyr Asp Ala Leu Tyr 435 440 445 Gln Trp Glu Arg Leu Gly Ser Leu Ala Val Thr Asn Ile Ser Leu Ala 450 455 460 Phe Phe Gln Asp Leu Val Pro Ser Ala Thr Val Gly Thr Tyr Ala Lys 465 470 475 480 Asp Thr Ile Thr Phe Ala Ser Ile Ser Ala Ala Val Arg Asp Tyr Ala 485 490 495 Asp Arg Phe Leu Arg Ile Val Gln Lys Tyr Thr Pro Pro Asn Gly Ala 500 505 510 Leu Ala Glu Gln Phe Ser Arg Tyr Asp Gly Ser Pro Leu Ser Ala Gln 515 520 525 Asp Leu Thr Trp Ser Tyr Thr Ser Phe Leu Thr Ala Val Gln Ala Arg 530 535 540 Arg His Ala Leu Asn Pro Ser Ala Ser His Ile Gln Pro Leu Leu Ser 545 550 555 560 Asn Ala Thr Thr Ala Thr Ala Leu Pro Gln Val Cys Thr Pro Ser Ser 565 570 575 Ala Arg Gly Pro Tyr Gln Pro Val Lys Arg Ile Lys Trp Pro Arg Pro 580 585 590 Glu Cys Leu Ser Pro Arg Ser Thr Val Ala Val Arg Phe Asn Val Leu 595 600 605 Ala Thr Thr Val Ile Gly Glu Asp Ile Phe Leu Val Gly Ser Ile Pro 610 615 620 Ala Leu Gly Glu Trp Asp Ala Arg His Gln Ala Leu Lys Leu Glu Ala 625 630 635 640 Asn Glu Tyr Ser Ser Ile Thr Pro Leu Trp Tyr Arg Thr Val Met Leu 645 650 655 Asp Ala Gly Glu Glu Phe Glu Tyr Lys Phe Ile Arg Lys Arg Val Gly 660 665 670 Asp Gly Lys Val Ile Trp Glu Glu Gly Gln Asn Arg Ala Phe Val Val 675 680 685 Pro Arg Glu Cys Gly Pro Ser Asn Ala Thr Ile Asn Ala Val Trp Arg 690 695 700 22 1455 DNA Aspergillus 22 atggtgactc tgactttcct gctttcggcg gcgtatctgc tttctgggtg agtggcttgg 60 atctattgct cggatagggc tgtggtgctg attctgaaac ggagtagagt gtctgcggca 120 cctagttctg ctggctccaa gtcctgcgat acggtagacc tcgggtacca gtgctcccct 180 gcgacttctc atctatgggg ccagtactcg ccattctttt cgctcgagga cgagctgtcc 240 gtgtcgagta agcttcccaa ggattgccgg atcaccttgg tacaggtgct atcgcgccat 300 ggagcgcggt acccaaccag ctccaagagc aaaaagtata agaagcttgt gacggcgatc 360 caggccaatg ccaccgactt caagggcaag tttgcctttt tgaagacgta caactatact 420 ctgggtgcgg atgacctcac tccctttggg gagcagcagc tggtgaactc gggcatcaag 480 ttctaccaga ggtacaaggc tctggcgcgc agtgtggtgc cgtttattcg cgcctcaggc 540 tcggaccggg ttattgcctc gggagagaag ttcatcgagg ggttccagca ggcgaagctg 600 gctgatcctg gcgcgacgaa ccgcgccgct ccggcgatta gtgtgattat tccggagagc 660 gagacgttca acaatacgct ggaccacggt gtgtgcacga agtttgaggc gagtcagctg 720 ggagatgagg ttgcggccaa tttcactgcg ctctttgcac ccgacatccg agctcgcgcc 780 gagaagcatc ttcctggcgt gacgctgaca gacgaggacg ttgtcagtct aatggacatg 840 tgttcgtttg atacggtagc gcgcaccagc gacgcaagtc agctgtcacc gttctgtcaa 900 ctcttcactc acaatgagtg gaagaagtac aactaccttc agtccttggg caagtactac 960 ggctacggcg caggcaaccc tctgggaccg gctcagggga tagggttcac caacgagctg 1020 attgcccggt tgactcgttc gccagtgcag gaccacacca gcactaactc gactctagtc 1080 tccaacccgg ccaccttccc gttgaacgct accatgtacg tcgacttttc acacgacaac 1140 agcatggttt ccatcttctt tgcattgggc ctgtacaacg gcactgaacc cttgtcccgg 1200 acctcggtgg aaagcgccaa ggaattggat gggtattctg catcctgggt ggtgcctttc 1260 ggcgcgcgag cctacttcga gacgatgcaa tgcaagtcgg aaaaggagcc tcttgttcgc 1320 gctttgatta atgaccgggt tgtgccactg catggctgcg atgtggacaa gctggggcga 1380 tgcaagctga atgactttgt caagggattg agttgggcca gatctggggg caactgggga 1440 gagtgcttta gttga 1455 23 1425 DNA Aspergillus CDS (1)...(1425) 23 atg gtg act ctg act ttc ctg ctt tcg gcg gcg tat ctg ctt tct ggg 48 Met Val Thr Leu Thr Phe Leu Leu Ser Ala Ala Tyr Leu Leu Ser Gly 1 5 10 15 gct gtg gtg ctg att ctg aaa cgg agt aga gtg tct gcg gca cct agt 96 Ala Val Val Leu Ile Leu Lys Arg Ser Arg Val Ser Ala Ala Pro Ser 20 25 30 tct gct ggc tcc aag tcc tgc gat acg gta gac ctc ggg tac cag tgc 144 Ser Ala Gly Ser Lys Ser Cys Asp Thr Val Asp Leu Gly Tyr Gln Cys 35 40 45 tcc cct gcg act tct cat cta tgg ggc cag tac tcg cca ttc ttt tcg 192 Ser Pro Ala Thr Ser His Leu Trp Gly Gln Tyr Ser Pro Phe Phe Ser 50 55 60 ctc gag gac gag ctg tcc gtg tcg agt aag ctt ccc aag gat tgc cgg 240 Leu Glu Asp Glu Leu Ser Val Ser Ser Lys Leu Pro Lys Asp Cys Arg 65 70 75 80 atc acc ttg gta cag gtg cta tcg cgc cat gga gcg cgg tac cca acc 288 Ile Thr Leu Val Gln Val Leu Ser Arg His Gly Ala Arg Tyr Pro Thr 85 90 95 agc tcc aag agc aaa aag tat aag aag ctt gtg acg gcg atc cag gcc 336 Ser Ser Lys Ser Lys Lys Tyr Lys Lys Leu Val Thr Ala Ile Gln Ala 100 105 110 aat gcc acc gac ttc aag ggc aag ttt gcc ttt ttg aag acg tac aac 384 Asn Ala Thr Asp Phe Lys Gly Lys Phe Ala Phe Leu Lys Thr Tyr Asn 115 120 125 tat act ctg ggt gcg gat gac ctc act ccc ttt ggg gag cag cag ctg 432 Tyr Thr Leu Gly Ala Asp Asp Leu Thr Pro Phe Gly Glu Gln Gln Leu 130 135 140 gtg aac tcg ggc atc aag ttc tac cag agg tac aag gct ctg gcg cgc 480 Val Asn Ser Gly Ile Lys Phe Tyr Gln Arg Tyr Lys Ala Leu Ala Arg 145 150 155 160 agt gtg gtg ccg ttt att cgc gcc tca ggc tcg gac cgg gtt att gcc 528 Ser Val Val Pro Phe Ile Arg Ala Ser Gly Ser Asp Arg Val Ile Ala 165 170 175 tcg gga gag aag ttc atc gag ggg ttc cag cag gcg aag ctg gct gat 576 Ser Gly Glu Lys Phe Ile Glu Gly Phe Gln Gln Ala Lys Leu Ala Asp 180 185 190 cct ggc gcg acg aac cgc gcc gct ccg gcg att agt gtg att att ccg 624 Pro Gly Ala Thr Asn Arg Ala Ala Pro Ala Ile Ser Val Ile Ile Pro 195 200 205 gag agc gag acg ttc aac aat acg ctg gac cac ggt gtg tgc acg aag 672 Glu Ser Glu Thr Phe Asn Asn Thr Leu Asp His Gly Val Cys Thr Lys 210 215 220 ttt gag gcg agt cag ctg gga gat gag gtt gcg gcc aat ttc act gcg 720 Phe Glu Ala Ser Gln Leu Gly Asp Glu Val Ala Ala Asn Phe Thr Ala 225 230 235 240 ctc ttt gca ccc gac atc cga gct cgc gcc gag aag cat ctt cct ggc 768 Leu Phe Ala Pro Asp Ile Arg Ala Arg Ala Glu Lys His Leu Pro Gly 245 250 255 gtg acg ctg aca gac gag gac gtt gtc agt cta atg gac atg tgt tcg 816 Val Thr Leu Thr Asp Glu Asp Val Val Ser Leu Met Asp Met Cys Ser 260 265 270 ttt gat acg gta gcg cgc acc agc gac gca agt cag ctg tca ccg ttc 864 Phe Asp Thr Val Ala Arg Thr Ser Asp Ala Ser Gln Leu Ser Pro Phe 275 280 285 tgt caa ctc ttc act cac aat gag tgg aag aag tac aac tac ctt cag 912 Cys Gln Leu Phe Thr His Asn Glu Trp Lys Lys Tyr Asn Tyr Leu Gln 290 295 300 tcc ttg ggc aag tac tac ggc tac ggc gca ggc aac cct ctg gga ccg 960 Ser Leu Gly Lys Tyr Tyr Gly Tyr Gly Ala Gly Asn Pro Leu Gly Pro 305 310 315 320 gct cag ggg ata ggg ttc acc aac gag ctg att gcc cgg ttg act cgt 1008 Ala Gln Gly Ile Gly Phe Thr Asn Glu Leu Ile Ala Arg Leu Thr Arg 325 330 335 tcg cca gtg cag gac cac acc agc act aac tcg act cta gtc tcc aac 1056 Ser Pro Val Gln Asp His Thr Ser Thr Asn Ser Thr Leu Val Ser Asn 340 345 350 ccg gcc acc ttc ccg ttg aac gct acc atg tac gtc gac ttt tca cac 1104 Pro Ala Thr Phe Pro Leu Asn Ala Thr Met Tyr Val Asp Phe Ser His 355 360 365 gac aac agc atg gtt tcc atc ttc ttt gca ttg ggc ctg tac aac ggc 1152 Asp Asn Ser Met Val Ser Ile Phe Phe Ala Leu Gly Leu Tyr Asn Gly 370 375 380 act gaa ccc ttg tcc cgg acc tcg gtg gaa agc gcc aag gaa ttg gat 1200 Thr Glu Pro Leu Ser Arg Thr Ser Val Glu Ser Ala Lys Glu Leu Asp 385 390 395 400 ggg tat tct gca tcc tgg gtg gtg cct ttc ggc gcg cga gcc tac ttc 1248 Gly Tyr Ser Ala Ser Trp Val Val Pro Phe Gly Ala Arg Ala Tyr Phe 405 410 415 gag acg atg caa tgc aag tcg gaa aag gag cct ctt gtt cgc gct ttg 1296 Glu Thr Met Gln Cys Lys Ser Glu Lys Glu Pro Leu Val Arg Ala Leu 420 425 430 att aat gac cgg gtt gtg cca ctg cat ggc tgc gat gtg gac aag ctg 1344 Ile Asn Asp Arg Val Val Pro Leu His Gly Cys Asp Val Asp Lys Leu 435 440 445 ggg cga tgc aag ctg aat gac ttt gtc aag gga ttg agt tgg gcc aga 1392 Gly Arg Cys Lys Leu Asn Asp Phe Val Lys Gly Leu Ser Trp Ala Arg 450 455 460 tct ggg ggc aac tgg gga gag tgc ttt agt tga 1425 Ser Gly Gly Asn Trp Gly Glu Cys Phe Ser * 465 470 24 474 PRT Aspergillus 24 Met Val Thr Leu Thr Phe Leu Leu Ser Ala Ala Tyr Leu Leu Ser Gly 1 5 10 15 Ala Val Val Leu Ile Leu Lys Arg Ser Arg Val Ser Ala Ala Pro Ser 20 25 30 Ser Ala Gly Ser Lys Ser Cys Asp Thr Val Asp Leu Gly Tyr Gln Cys 35 40 45 Ser Pro Ala Thr Ser His Leu Trp Gly Gln Tyr Ser Pro Phe Phe Ser 50 55 60 Leu Glu Asp Glu Leu Ser Val Ser Ser Lys Leu Pro Lys Asp Cys Arg 65 70 75 80 Ile Thr Leu Val Gln Val Leu Ser Arg His Gly Ala Arg Tyr Pro Thr 85 90 95 Ser Ser Lys Ser Lys Lys Tyr Lys Lys Leu Val Thr Ala Ile Gln Ala 100 105 110 Asn Ala Thr Asp Phe Lys Gly Lys Phe Ala Phe Leu Lys Thr Tyr Asn 115 120 125 Tyr Thr Leu Gly Ala Asp Asp Leu Thr Pro Phe Gly Glu Gln Gln Leu 130 135 140 Val Asn Ser Gly Ile Lys Phe Tyr Gln Arg Tyr Lys Ala Leu Ala Arg 145 150 155 160 Ser Val Val Pro Phe Ile Arg Ala Ser Gly Ser Asp Arg Val Ile Ala 165 170 175 Ser Gly Glu Lys Phe Ile Glu Gly Phe Gln Gln Ala Lys Leu Ala Asp 180 185 190 Pro Gly Ala Thr Asn Arg Ala Ala Pro Ala Ile Ser Val Ile Ile Pro 195 200 205 Glu Ser Glu Thr Phe Asn Asn Thr Leu Asp His Gly Val Cys Thr Lys 210 215 220 Phe Glu Ala Ser Gln Leu Gly Asp Glu Val Ala Ala Asn Phe Thr Ala 225 230 235 240 Leu Phe Ala Pro Asp Ile Arg Ala Arg Ala Glu Lys His Leu Pro Gly 245 250 255 Val Thr Leu Thr Asp Glu Asp Val Val Ser Leu Met Asp Met Cys Ser 260 265 270 Phe Asp Thr Val Ala Arg Thr Ser Asp Ala Ser Gln Leu Ser Pro Phe 275 280 285 Cys Gln Leu Phe Thr His Asn Glu Trp Lys Lys Tyr Asn Tyr Leu Gln 290 295 300 Ser Leu Gly Lys Tyr Tyr Gly Tyr Gly Ala Gly Asn Pro Leu Gly Pro 305 310 315 320 Ala Gln Gly Ile Gly Phe Thr Asn Glu Leu Ile Ala Arg Leu Thr Arg 325 330 335 Ser Pro Val Gln Asp His Thr Ser Thr Asn Ser Thr Leu Val Ser Asn 340 345 350 Pro Ala Thr Phe Pro Leu Asn Ala Thr Met Tyr Val Asp Phe Ser His 355 360 365 Asp Asn Ser Met Val Ser Ile Phe Phe Ala Leu Gly Leu Tyr Asn Gly 370 375 380 Thr Glu Pro Leu Ser Arg Thr Ser Val Glu Ser Ala Lys Glu Leu Asp 385 390 395 400 Gly Tyr Ser Ala Ser Trp Val Val Pro Phe Gly Ala Arg Ala Tyr Phe 405 410 415 Glu Thr Met Gln Cys Lys Ser Glu Lys Glu Pro Leu Val Arg Ala Leu 420 425 430 Ile Asn Asp Arg Val Val Pro Leu His Gly Cys Asp Val Asp Lys Leu 435 440 445 Gly Arg Cys Lys Leu Asn Asp Phe Val Lys Gly Leu Ser Trp Ala Arg 450 455 460 Ser Gly Gly Asn Trp Gly Glu Cys Phe Ser 465 470 25 2997 DNA Aspergillus 25 atgaagtccc ttttaaagag attgattgca ctggccgccg cttattcggt agcagctgca 60 ccatccttta gccaccattc atctcaagat gctgcgaata agagagagct tcttcaagac 120 ttagtgacgt gggaccaaca ctccctgttt gtccggggcg agcggctcat gatcttctct 180 ggagagtttc acccttttcg actgccagtt cctggactct ggtttgatgt cttccagaag 240 attaagagtc tgggattcaa tgctgtctcc ttctatactg actggggtct catggagggt 300 aatcctggcc acgttgtgac tgacggtatc tggagccttg acgagttttt cactgctgca 360 cgtgaagccg gtctctacct gatcgctcgg ccagggccat atatcaatgc ggaaacctcg 420 gctggtggta tacccggatg ggttctccgt cgaaagggca tcatccgctc aaacagtgag 480 gattacctcc gtgcgacaga tacgtacatg gccactctag ggaagataat tgccaaggcg 540 caaattacca atggagggcc ggtgatcttg gttcagccag aaaatgagta cacgacttgg 600 cccaacgtct cagagtccga gtttccgacg accatgaatc aggaagtcat ggcctatgcc 660 gagaagcagc ttcgagacgc tggagtagtt gttccaaccg ttgtaaatga caataagaac 720 ctgggatact ttgcccctgg gactggactg ggcgagacgg atctctacgg gattgacgcc 780 tatcctatga gatatgactg tgagaccatt actttcaaga gatgattgga tctgatgcag 840 aatcaggtgg taacccctat gtatggccaa catatcgatt cccgcgagat tggcagcatg 900 aacaccgcaa ccatagccct acaacgccat ttgctattat ggagttccaa gggggttcag 960 gggatgggtg gtaagagata cataccatgg gtactgcccc tatgaacgca atgactaaca 1020 taatcaccag gggaggagtc acagaagacg gatgtgccat tcttgtcaac aatgaagctg 1080 tgcgagtggt gtacaagaac aattacggat ttggcgtcag agtgttcaac atctacatgg 1140 tgtgaaatgc tccctcctcc tcctccctac atccgctcct aactgactgt gtagacgtac 1200 ggaggcacca attggggcaa tctcggctac tatggaggat acacctcgta tgactacggg 1260 gctgccatta ccgaggatcg tcagatctgg cgagaaaagt atagcgaaga gaagctacag 1320 gcaaactttc tgaaagtgtc tccggcgtac ctcacctcaa cgcctggaaa cggggtcaat 1380 ggatcataca caggaaacaa ggatataacg gtcactccgt tgtttggcaa tggaacgacc 1440 accaatctct atctagtccg gcatgccgac tttacttcga ctggaagtgc ccaatacaat 1500 ctcagcattt ccacgagcgt cggaaatgtg acgatccctc aactaggagg cagtctctcc 1560 ttgaacggcc gagactccaa attccacatc acggactatg atgtgggtgg attcaatctc 1620 atctactctt ctgcagaagt cttcacttgg gcgaagggag acaacaagaa gcgcgttctc 1680 gtgctatatg gaggagcagg ggaactacat gagttcgcgc tgcccaaaca tcttccgcgg 1740 ccaaccgttg ttgaggggtc ctacgtcaag attgccaaac agggaagtgc ctgggtcgta 1800 cagtgggagg tagctgctca aagacgggtt ttacgtgcag gaaagcttga gatccacctc 1860 ctctggcgta acgacgccta ccagcactgg gtcttggaac taccagcaaa acaacccatt 1920 gctaactata gctcgccatc caaagagacg gtgattgtga agggaggata tttgcttcga 1980 agcgcgtgga ttactgacaa tgacctgcat ttgactggtg atgtgaacgt aacaactccc 2040 ttggaggtga tttcagcgcc gaagcgattt gatgggattg tcttcaacgg ccagtccttg 2100 aaatcaacac gatctaagat tggcaatctc gctgcaacag ttcactatca accaccagct 2160 atctctctgc cagatctaaa gcgtcttgac tggaaataca tcgattctct cccagagatc 2220 tccacggaat ataacgacga gggctggaca ccactgacga acacatacac caataacacc 2280 agagagttca ctggccctac atgtctgtac gccgatgact acggctatca cgggggctca 2340 ctgatctacc ggggccactt cacggccaac ggagacgagt catgggtttt cctcaacacc 2400 tctggcggtg taggcttcgc caattcggta tggctaaacc aaacattcct gggttcatgg 2460 acaggcagtg gaagaaacat gacctatccc cgaaacatct cgcttcccca cgagctgtct 2520 cctggggaac cgtacgtttt caccgtggtg atcgaccaca tgggccagga cgaagaggca 2580 ccggggacag acgcaatcaa gtttcctcga ggaattctcg actacgcgct ctcgggccat 2640 gagctgtccg atctccgatg gaagatgact ggcaacctcg gcggcgagca gtaccaggat 2700 ttgacgcgag gtccgctcaa cgagggagcc atgtatgccg agcggcaggg atatcatctt 2760 ccaagtccgc ctacttccag ctggaagtca tccaacccga ttaaggaagg gctcactggc 2820 gctggtattg gattctatgc tacttcgttc tccttggatc tacccgaggg atacgatatc 2880 ccattgagct ttcggttcaa caactcggca tcagccgcga ggtcagggac gagctatcgc 2940 tgtcagctgt ttgttaatgg ataccagttt ggaaaatacg gtatgataag aagttga 2997 26 2835 DNA Aspergillus CDS (1)...(2835) 26 atg aag tcc ctt tta aag aga ttg att gca ctg gcc gcc gct tat tcg 48 Met Lys Ser Leu Leu Lys Arg Leu Ile Ala Leu Ala Ala Ala Tyr Ser 1 5 10 15 gta gca gct gca cca tcc ttt agc cac cat tca tct caa gat gct gcg 96 Val Ala Ala Ala Pro Ser Phe Ser His His Ser Ser Gln Asp Ala Ala 20 25 30 aat aag aga gag ctt ctt caa gac tta gtg acg tgg gac caa cac tcc 144 Asn Lys Arg Glu Leu Leu Gln Asp Leu Val Thr Trp Asp Gln His Ser 35 40 45 ctg ttt gtc cgg ggc gag cgg ctc atg atc ttc tct gga gag ttt cac 192 Leu Phe Val Arg Gly Glu Arg Leu Met Ile Phe Ser Gly Glu Phe His 50 55 60 cct ttt cga ctg cca gtt cct gga ctc tgg ttt gat gtc ttc cag aag 240 Pro Phe Arg Leu Pro Val Pro Gly Leu Trp Phe Asp Val Phe Gln Lys 65 70 75 80 att aag agt ctg gga ttc aat gct gtc tcc ttc tat act gac tgg ggt 288 Ile Lys Ser Leu Gly Phe Asn Ala Val Ser Phe Tyr Thr Asp Trp Gly 85 90 95 ctc atg gag ggt aat cct ggc cac gtt gtg act gac ggt atc tgg agc 336 Leu Met Glu Gly Asn Pro Gly His Val Val Thr Asp Gly Ile Trp Ser 100 105 110 ctt gac gag ttt ttc act gct gca cgt gaa gcc ggt ctc tac ctg atc 384 Leu Asp Glu Phe Phe Thr Ala Ala Arg Glu Ala Gly Leu Tyr Leu Ile 115 120 125 gct cgg cca ggg cca tat atc aat gcg gaa acc tcg gct ggt ggt ata 432 Ala Arg Pro Gly Pro Tyr Ile Asn Ala Glu Thr Ser Ala Gly Gly Ile 130 135 140 ccc gga tgg gtt ctc cgt cga aag ggc atc atc cgc tca aac agt gag 480 Pro Gly Trp Val Leu Arg Arg Lys Gly Ile Ile Arg Ser Asn Ser Glu 145 150 155 160 gat tac ctc cgt gcg aca gat acg tac atg gcc act cta ggg aag ata 528 Asp Tyr Leu Arg Ala Thr Asp Thr Tyr Met Ala Thr Leu Gly Lys Ile 165 170 175 att gcc aag gcg caa att acc aat gga ggg ccg gtg atc ttg gtt cag 576 Ile Ala Lys Ala Gln Ile Thr Asn Gly Gly Pro Val Ile Leu Val Gln 180 185 190 cca gaa aat gag tac acg act tgg ccc aac gtc tca gag tcc gag ttt 624 Pro Glu Asn Glu Tyr Thr Thr Trp Pro Asn Val Ser Glu Ser Glu Phe 195 200 205 ccg acg acc atg aat cag gaa gtc atg gcc tat gcc gag aag cag ctt 672 Pro Thr Thr Met Asn Gln Glu Val Met Ala Tyr Ala Glu Lys Gln Leu 210 215 220 cga gac gct gga gta gtt gtt cca acc gtt gta aat gac aat aag aac 720 Arg Asp Ala Gly Val Val Val Pro Thr Val Val Asn Asp Asn Lys Asn 225 230 235 240 ctg gga tac ttt gcc cct ggg act gga ctg ggc gag acg gat ctc tac 768 Leu Gly Tyr Phe Ala Pro Gly Thr Gly Leu Gly Glu Thr Asp Leu Tyr 245 250 255 ggg att gac gcc tat cct atg aga tat gac tgt ggt aac ccc tat gta 816 Gly Ile Asp Ala Tyr Pro Met Arg Tyr Asp Cys Gly Asn Pro Tyr Val 260 265 270 tgg cca aca tat cga ttc ccg cga gat tgg cag cat gaa cac cgc aac 864 Trp Pro Thr Tyr Arg Phe Pro Arg Asp Trp Gln His Glu His Arg Asn 275 280 285 cat agc cct aca acg cca ttt gct att atg gag ttc caa ggg ggt tca 912 His Ser Pro Thr Thr Pro Phe Ala Ile Met Glu Phe Gln Gly Gly Ser 290 295 300 ggg gat ggg tgg gga gga gtc aca gaa gac gga tgt gcc att ctt gtc 960 Gly Asp Gly Trp Gly Gly Val Thr Glu Asp Gly Cys Ala Ile Leu Val 305 310 315 320 aac aat gaa gct gtg cga gtg gtg tac aag aac aat tac gga ttt ggc 1008 Asn Asn Glu Ala Val Arg Val Val Tyr Lys Asn Asn Tyr Gly Phe Gly 325 330 335 gtc aga gtg ttc aac atc tac atg acg tac gga ggc acc aat tgg ggc 1056 Val Arg Val Phe Asn Ile Tyr Met Thr Tyr Gly Gly Thr Asn Trp Gly 340 345 350 aat ctc ggc tac tat gga gga tac acc tcg tat gac tac ggg gct gcc 1104 Asn Leu Gly Tyr Tyr Gly Gly Tyr Thr Ser Tyr Asp Tyr Gly Ala Ala 355 360 365 att acc gag gat cgt cag atc tgg cga gaa aag tat agc gaa gag aag 1152 Ile Thr Glu Asp Arg Gln Ile Trp Arg Glu Lys Tyr Ser Glu Glu Lys 370 375 380 cta cag gca aac ttt ctg aaa gtg tct ccg gcg tac ctc acc tca acg 1200 Leu Gln Ala Asn Phe Leu Lys Val Ser Pro Ala Tyr Leu Thr Ser Thr 385 390 395 400 cct gga aac ggg gtc aat gga tca tac aca gga aac aag gat ata acg 1248 Pro Gly Asn Gly Val Asn Gly Ser Tyr Thr Gly Asn Lys Asp Ile Thr 405 410 415 gtc act ccg ttg ttt ggc aat gga acg acc acc aat ctc tat cta gtc 1296 Val Thr Pro Leu Phe Gly Asn Gly Thr Thr Thr Asn Leu Tyr Leu Val 420 425 430 cgg cat gcc gac ttt act tcg act gga agt gcc caa tac aat ctc agc 1344 Arg His Ala Asp Phe Thr Ser Thr Gly Ser Ala Gln Tyr Asn Leu Ser 435 440 445 att tcc acg agc gtc gga aat gtg acg atc cct caa cta gga ggc agt 1392 Ile Ser Thr Ser Val Gly Asn Val Thr Ile Pro Gln Leu Gly Gly Ser 450 455 460 ctc tcc ttg aac ggc cga gac tcc aaa ttc cac atc acg gac tat gat 1440 Leu Ser Leu Asn Gly Arg Asp Ser Lys Phe His Ile Thr Asp Tyr Asp 465 470 475 480 gtg ggt gga ttc aat ctc atc tac tct tct gca gaa gtc ttc act tgg 1488 Val Gly Gly Phe Asn Leu Ile Tyr Ser Ser Ala Glu Val Phe Thr Trp 485 490 495 gcg aag gga gac aac aag aag cgc gtt ctc gtg cta tat gga gga gca 1536 Ala Lys Gly Asp Asn Lys Lys Arg Val Leu Val Leu Tyr Gly Gly Ala 500 505 510 ggg gaa cta cat gag ttc gcg ctg ccc aaa cat ctt ccg cgg cca acc 1584 Gly Glu Leu His Glu Phe Ala Leu Pro Lys His Leu Pro Arg Pro Thr 515 520 525 gtt gtt gag ggg tcc tac gtc aag att gcc aaa cag gga agt gcc tgg 1632 Val Val Glu Gly Ser Tyr Val Lys Ile Ala Lys Gln Gly Ser Ala Trp 530 535 540 gtc gta cag tgg gag gta gct gct caa aga cgg gtt tta cgt gca gga 1680 Val Val Gln Trp Glu Val Ala Ala Gln Arg Arg Val Leu Arg Ala Gly 545 550 555 560 aag ctt gag atc cac ctc ctc tgg cgt aac gac gcc tac cag cac tgg 1728 Lys Leu Glu Ile His Leu Leu Trp Arg Asn Asp Ala Tyr Gln His Trp 565 570 575 gtc ttg gaa cta cca gca aaa caa ccc att gct aac tat agc tcg cca 1776 Val Leu Glu Leu Pro Ala Lys Gln Pro Ile Ala Asn Tyr Ser Ser Pro 580 585 590 tcc aaa gag acg gtg att gtg aag gga gga tat ttg ctt cga agc gcg 1824 Ser Lys Glu Thr Val Ile Val Lys Gly Gly Tyr Leu Leu Arg Ser Ala 595 600 605 tgg att act gac aat gac ctg cat ttg act ggt gat gtg aac gta aca 1872 Trp Ile Thr Asp Asn Asp Leu His Leu Thr Gly Asp Val Asn Val Thr 610 615 620 act ccc ttg gag gtg att tca gcg ccg aag cga ttt gat ggg att gtc 1920 Thr Pro Leu Glu Val Ile Ser Ala Pro Lys Arg Phe Asp Gly Ile Val 625 630 635 640 ttc aac ggc cag tcc ttg aaa tca aca cga tct aag att ggc aat ctc 1968 Phe Asn Gly Gln Ser Leu Lys Ser Thr Arg Ser Lys Ile Gly Asn Leu 645 650 655 gct gca aca gtt cac tat caa cca cca gct atc tct ctg cca gat cta 2016 Ala Ala Thr Val His Tyr Gln Pro Pro Ala Ile Ser Leu Pro Asp Leu 660 665 670 aag cgt ctt gac tgg aaa tac atc gat tct ctc cca gag atc tcc acg 2064 Lys Arg Leu Asp Trp Lys Tyr Ile Asp Ser Leu Pro Glu Ile Ser Thr 675 680 685 gaa tat aac gac gag ggc tgg aca cca ctg acg aac aca tac acc aat 2112 Glu Tyr Asn Asp Glu Gly Trp Thr Pro Leu Thr Asn Thr Tyr Thr Asn 690 695 700 aac acc aga gag ttc act ggc cct aca tgt ctg tac gcc gat gac tac 2160 Asn Thr Arg Glu Phe Thr Gly Pro Thr Cys Leu Tyr Ala Asp Asp Tyr 705 710 715 720 ggc tat cac ggg ggc tca ctg atc tac cgg ggc cac ttc acg gcc aac 2208 Gly Tyr His Gly Gly Ser Leu Ile Tyr Arg Gly His Phe Thr Ala Asn 725 730 735 gga gac gag tca tgg gtt ttc ctc aac acc tct ggc ggt gta ggc ttc 2256 Gly Asp Glu Ser Trp Val Phe Leu Asn Thr Ser Gly Gly Val Gly Phe 740 745 750 gcc aat tcg gta tgg cta aac caa aca ttc ctg ggt tca tgg aca ggc 2304 Ala Asn Ser Val Trp Leu Asn Gln Thr Phe Leu Gly Ser Trp Thr Gly 755 760 765 agt gga aga aac atg acc tat ccc cga aac atc tcg ctt ccc cac gag 2352 Ser Gly Arg Asn Met Thr Tyr Pro Arg Asn Ile Ser Leu Pro His Glu 770 775 780 ctg tct cct ggg gaa ccg tac gtt ttc acc gtg gtg atc gac cac atg 2400 Leu Ser Pro Gly Glu Pro Tyr Val Phe Thr Val Val Ile Asp His Met 785 790 795 800 ggc cag gac gaa gag gca ccg ggg aca gac gca atc aag ttt cct cga 2448 Gly Gln Asp Glu Glu Ala Pro Gly Thr Asp Ala Ile Lys Phe Pro Arg 805 810 815 gga att ctc gac tac gcg ctc tcg ggc cat gag ctg tcc gat ctc cga 2496 Gly Ile Leu Asp Tyr Ala Leu Ser Gly His Glu Leu Ser Asp Leu Arg 820 825 830 tgg aag atg act ggc aac ctc ggc ggc gag cag tac cag gat ttg acg 2544 Trp Lys Met Thr Gly Asn Leu Gly Gly Glu Gln Tyr Gln Asp Leu Thr 835 840 845 cga ggt ccg ctc aac gag gga gcc atg tat gcc gag cgg cag gga tat 2592 Arg Gly Pro Leu Asn Glu Gly Ala Met Tyr Ala Glu Arg Gln Gly Tyr 850 855 860 cat ctt cca agt ccg cct act tcc agc tgg aag tca tcc aac ccg att 2640 His Leu Pro Ser Pro Pro Thr Ser Ser Trp Lys Ser Ser Asn Pro Ile 865 870 875 880 aag gaa ggg ctc act ggc gct ggt att gga ttc tat gct act tcg ttc 2688 Lys Glu Gly Leu Thr Gly Ala Gly Ile Gly Phe Tyr Ala Thr Ser Phe 885 890 895 tcc ttg gat cta ccc gag gga tac gat atc cca ttg agc ttt cgg ttc 2736 Ser Leu Asp Leu Pro Glu Gly Tyr Asp Ile Pro Leu Ser Phe Arg Phe 900 905 910 aac aac tcg gca tca gcc gcg agg tca ggg acg agc tat cgc tgt cag 2784 Asn Asn Ser Ala Ser Ala Ala Arg Ser Gly Thr Ser Tyr Arg Cys Gln 915 920 925 ctg ttt gtt aat gga tac cag ttt gga aaa tac ggt atg ata aga agt 2832 Leu Phe Val Asn Gly Tyr Gln Phe Gly Lys Tyr Gly Met Ile Arg Ser 930 935 940 tga 2835 * 27 944 PRT Aspergillus 27 Met Lys Ser Leu Leu Lys Arg Leu Ile Ala Leu Ala Ala Ala Tyr Ser 1 5 10 15 Val Ala Ala Ala Pro Ser Phe Ser His His Ser Ser Gln Asp Ala Ala 20 25 30 Asn Lys Arg Glu Leu Leu Gln Asp Leu Val Thr Trp Asp Gln His Ser 35 40 45 Leu Phe Val Arg Gly Glu Arg Leu Met Ile Phe Ser Gly Glu Phe His 50 55 60 Pro Phe Arg Leu Pro Val Pro Gly Leu Trp Phe Asp Val Phe Gln Lys 65 70 75 80 Ile Lys Ser Leu Gly Phe Asn Ala Val Ser Phe Tyr Thr Asp Trp Gly 85 90 95 Leu Met Glu Gly Asn Pro Gly His Val Val Thr Asp Gly Ile Trp Ser 100 105 110 Leu Asp Glu Phe Phe Thr Ala Ala Arg Glu Ala Gly Leu Tyr Leu Ile 115 120 125 Ala Arg Pro Gly Pro Tyr Ile Asn Ala Glu Thr Ser Ala Gly Gly Ile 130 135 140 Pro Gly Trp Val Leu Arg Arg Lys Gly Ile Ile Arg Ser Asn Ser Glu 145 150 155 160 Asp Tyr Leu Arg Ala Thr Asp Thr Tyr Met Ala Thr Leu Gly Lys Ile 165 170 175 Ile Ala Lys Ala Gln Ile Thr Asn Gly Gly Pro Val Ile Leu Val Gln 180 185 190 Pro Glu Asn Glu Tyr Thr Thr Trp Pro Asn Val Ser Glu Ser Glu Phe 195 200 205 Pro Thr Thr Met Asn Gln Glu Val Met Ala Tyr Ala Glu Lys Gln Leu 210 215 220 Arg Asp Ala Gly Val Val Val Pro Thr Val Val Asn Asp Asn Lys Asn 225 230 235 240 Leu Gly Tyr Phe Ala Pro Gly Thr Gly Leu Gly Glu Thr Asp Leu Tyr 245 250 255 Gly Ile Asp Ala Tyr Pro Met Arg Tyr Asp Cys Gly Asn Pro Tyr Val 260 265 270 Trp Pro Thr Tyr Arg Phe Pro Arg Asp Trp Gln His Glu His Arg Asn 275 280 285 His Ser Pro Thr Thr Pro Phe Ala Ile Met Glu Phe Gln Gly Gly Ser 290 295 300 Gly Asp Gly Trp Gly Gly Val Thr Glu Asp Gly Cys Ala Ile Leu Val 305 310 315 320 Asn Asn Glu Ala Val Arg Val Val Tyr Lys Asn Asn Tyr Gly Phe Gly 325 330 335 Val Arg Val Phe Asn Ile Tyr Met Thr Tyr Gly Gly Thr Asn Trp Gly 340 345 350 Asn Leu Gly Tyr Tyr Gly Gly Tyr Thr Ser Tyr Asp Tyr Gly Ala Ala 355 360 365 Ile Thr Glu Asp Arg Gln Ile Trp Arg Glu Lys Tyr Ser Glu Glu Lys 370 375 380 Leu Gln Ala Asn Phe Leu Lys Val Ser Pro Ala Tyr Leu Thr Ser Thr 385 390 395 400 Pro Gly Asn Gly Val Asn Gly Ser Tyr Thr Gly Asn Lys Asp Ile Thr 405 410 415 Val Thr Pro Leu Phe Gly Asn Gly Thr Thr Thr Asn Leu Tyr Leu Val 420 425 430 Arg His Ala Asp Phe Thr Ser Thr Gly Ser Ala Gln Tyr Asn Leu Ser 435 440 445 Ile Ser Thr Ser Val Gly Asn Val Thr Ile Pro Gln Leu Gly Gly Ser 450 455 460 Leu Ser Leu Asn Gly Arg Asp Ser Lys Phe His Ile Thr Asp Tyr Asp 465 470 475 480 Val Gly Gly Phe Asn Leu Ile Tyr Ser Ser Ala Glu Val Phe Thr Trp 485 490 495 Ala Lys Gly Asp Asn Lys Lys Arg Val Leu Val Leu Tyr Gly Gly Ala 500 505 510 Gly Glu Leu His Glu Phe Ala Leu Pro Lys His Leu Pro Arg Pro Thr 515 520 525 Val Val Glu Gly Ser Tyr Val Lys Ile Ala Lys Gln Gly Ser Ala Trp 530 535 540 Val Val Gln Trp Glu Val Ala Ala Gln Arg Arg Val Leu Arg Ala Gly 545 550 555 560 Lys Leu Glu Ile His Leu Leu Trp Arg Asn Asp Ala Tyr Gln His Trp 565 570 575 Val Leu Glu Leu Pro Ala Lys Gln Pro Ile Ala Asn Tyr Ser Ser Pro 580 585 590 Ser Lys Glu Thr Val Ile Val Lys Gly Gly Tyr Leu Leu Arg Ser Ala 595 600 605 Trp Ile Thr Asp Asn Asp Leu His Leu Thr Gly Asp Val Asn Val Thr 610 615 620 Thr Pro Leu Glu Val Ile Ser Ala Pro Lys Arg Phe Asp Gly Ile Val 625 630 635 640 Phe Asn Gly Gln Ser Leu Lys Ser Thr Arg Ser Lys Ile Gly Asn Leu 645 650 655 Ala Ala Thr Val His Tyr Gln Pro Pro Ala Ile Ser Leu Pro Asp Leu 660 665 670 Lys Arg Leu Asp Trp Lys Tyr Ile Asp Ser Leu Pro Glu Ile Ser Thr 675 680 685 Glu Tyr Asn Asp Glu Gly Trp Thr Pro Leu Thr Asn Thr Tyr Thr Asn 690 695 700 Asn Thr Arg Glu Phe Thr Gly Pro Thr Cys Leu Tyr Ala Asp Asp Tyr 705 710 715 720 Gly Tyr His Gly Gly Ser Leu Ile Tyr Arg Gly His Phe Thr Ala Asn 725 730 735 Gly Asp Glu Ser Trp Val Phe Leu Asn Thr Ser Gly Gly Val Gly Phe 740 745 750 Ala Asn Ser Val Trp Leu Asn Gln Thr Phe Leu Gly Ser Trp Thr Gly 755 760 765 Ser Gly Arg Asn Met Thr Tyr Pro Arg Asn Ile Ser Leu Pro His Glu 770 775 780 Leu Ser Pro Gly Glu Pro Tyr Val Phe Thr Val Val Ile Asp His Met 785 790 795 800 Gly Gln Asp Glu Glu Ala Pro Gly Thr Asp Ala Ile Lys Phe Pro Arg 805 810 815 Gly Ile Leu Asp Tyr Ala Leu Ser Gly His Glu Leu Ser Asp Leu Arg 820 825 830 Trp Lys Met Thr Gly Asn Leu Gly Gly Glu Gln Tyr Gln Asp Leu Thr 835 840 845 Arg Gly Pro Leu Asn Glu Gly Ala Met Tyr Ala Glu Arg Gln Gly Tyr 850 855 860 His Leu Pro Ser Pro Pro Thr Ser Ser Trp Lys Ser Ser Asn Pro Ile 865 870 875 880 Lys Glu Gly Leu Thr Gly Ala Gly Ile Gly Phe Tyr Ala Thr Ser Phe 885 890 895 Ser Leu Asp Leu Pro Glu Gly Tyr Asp Ile Pro Leu Ser Phe Arg Phe 900 905 910 Asn Asn Ser Ala Ser Ala Ala Arg Ser Gly Thr Ser Tyr Arg Cys Gln 915 920 925 Leu Phe Val Asn Gly Tyr Gln Phe Gly Lys Tyr Gly Met Ile Arg Ser 930 935 940 28 3433 DNA Aspergillus 28 atgaagcttc tctctgtctg cgcaattgcc ttgttggcag ctcaggcagc gggtgcttcc 60 atcaagcaca tgctcaatgg cttcactctt atggagcact cggatcctgc gaagcgggaa 120 ctgctacaga aatacgtatg tgggatcgaa aacttggtaa tcgattaatg tgtactcaga 180 catagctcta ggtcacctgg gatgagaagt cactgtttgt caatggcgag agaatcatga 240 ttttcagcgg cgaagttcac cctttcaggt gcgacacaga cgcggtgatc tactctggtt 300 tgttcttaca ttcttacatt gtgtagactg cccgttcctt cgctgtggct cgatgtcttt 360 cagaaaatca aggccctggg gttcaattgc gtttcattct acgtcgactg ggccctcctc 420 gaaggaaaac ctggcgagta cagggctgaa ggcaactttg ccctcgagcc tttctttgac 480 gtggctaagc aggcaggaat ctatctcctc gctcgtcctg gaccttatat caatgctgag 540 gcttcgggcg gtggtttccc tggatggttg cagagagtga acggaaccct gcggacatcc 600 gatcccgcgt acctgaaggc tactgataag tatgtcgcgt acgattgttt gtagcctcga 660 agctgctaac tctgaatcag ctacattgcc catgttgctg ctactattgc caaaggccaa 720 atcacaaacg ggggccccgt cattctttat caaccggaga atgagtacag cggggcgtgt 780 tgtgatgcta ctttccccga tggggactac atgcaatatg tcatcgacca ggctcgaaac 840 gccggtattg ttgtaccatt gatcaataac gatgcctgga ctggaggaca caatgcccct 900 gggacgggca agggcgaggt tgacatctat ggtcacgata gctatccgtg agtcaaattc 960 caccttctgg gaagacaatc ctaacttgct ttgattagac taggatttga ctgtgtaaga 1020 ttgagttttg ttgaactctt tgagcgattc tgatgaaaat agggacaccc aagcgtttgg 1080 cccaagggca acctgccaac cactttccgg acggatcact tgaagcagag cccgacaacc 1140 ccgtactctc ttattgaggt gtgtgtgtgt ctcaaatgcc ctcggatccg gacaccacta 1200 atcgtcgtgc agttccaagc aggttccttt gatccatggg gtggacccgg ctttgcagca 1260 tgcgccgccc tcgtcaatca cgagttcgag agagtattct acaagaatga cctaagcttt 1320 ggagctgcta tcctgaactt gtacatggta tggaaggatc ccgcttaaga ttgaccaagc 1380 gctgacacgc ttagaccttt ggcggcacga actggggtaa ccttggccat cccggtggat 1440 acacatccta cgattatgga tcgccgctga ctgaatctcg caatgtcact cgagagaagt 1500 acagtgagct caagttaatc ggtaacttcg tgaaagcctc gccgtcttac cttctggcta 1560 cgcctggcaa tttgactacc tctggatatg ccgacaccgc tgatttgacc gtgactcctt 1620 tgctgggcaa tggcactgga tcgtactttg ttgtcagaca tacggattac accagccagg 1680 catctacccc gtacaaactc agcctcccaa ccagtgctgg aagactcaca gttccccagc 1740 tcggcggtac tctgacgctc aatggacgtg attccaaaat tcatgttgtg gactacaacg 1800 tcgcggggac caatatcata tactcgactg ccgaagtctt cacctggaag aactttgggg 1860 atagcaaagt cctcatcttg tatggtggac ctggcgagca ccatgagctg gcggtttctt 1920 tcaagtccga cgtccaggtc gtcgaaggat ctaattcaga attcaagtcg aagaaggtgg 1980 gggatgttgc tgtggttgcc tgggatgtgt ctccatcccg ccgtattgtc cagattggcg 2040 acctcaagat attcctgctg ggtgagtaga tccgcttgtt cttcttactc aaagctgatt 2100 tcgagcagat aggaactctg tctacaatta ctgggtgcca caacttgaca aggacgactc 2160 gtcaacgggc tacagctccg aaaagactac tgcttcgtcc attattgtca aggctggtta 2220 ccttgtgcga accgcttata ctaagggctc cggcctctat cttactgctg acttcaacgc 2280 aacaactcct gtcgaagtga tcggagcccc gtcaaacgtc cggaacctgt acatcaacgg 2340 cgagaagacc cagttcaaga ccgataagaa tggtatctgg tcaactgagg tcaagtacag 2400 tgctcctaag atcaagcttc ccagcatgaa ggatctggat tggaagtatc ttgatactct 2460 gcaggaggtt cagtcaacct atgacgattc tgcgtggcca gcagccgacc tggacaccac 2520 acctaacacc ttgcgaccct tgaccacgcc aaagtctctg tactcgtcgg actatggctt 2580 ccatacgggt tacctgatct accgcggcca ctttgttgct gacggcagcg agactacatt 2640 tgacgtgcgc acgcaaggag gctcggcctt tggcagttcc gtctggctga acgaatcatt 2700 cctaggctcc tggactggtc tcaacgccaa tgcggactac aactcaacct acaaattgcc 2760 gcaggtcgag caaggcaaga actatgtcct cactattctc attgacacaa tgggcctcaa 2820 cgagaactgg gttgtcggca cggacgagat gaagaacccc cggggtattc tctcctacaa 2880 gctctccggc cgggacgcct ccgccatcac ctggaaattg accggaaacc tcggcggaga 2940 ggattaccaa gacaagatcc gcggccctct gaacgaaggt ggattgtatg ccgaacggca 3000 aggcttccac cagccccagc cgcccagcca gaagtggaaa tcagctagtc ctctcgatgg 3060 gttatccaag cctggcattg gcttctacac cgctcagttt gatctggata tcccaagcgg 3120 gtgggacgtg ccgctctact tcaactttgg caacagcacg aagtcagcct accgggtgca 3180 gctgtatgtc aacggatacc agtacggcaa gttcgtcagc aacataggcc ctcagacaag 3240 cttccccgtc ccgcagggta tcctgaacta tcagggaacc aattgggttg cgttgactct 3300 ctgggcactc gagtcggatg gtgccaagtt ggatgacttt gagttggtga acaccacacc 3360 agtcatgact gccctatcaa aaattcggcc atcaaagcag ccaaattatc gtcaacggaa 3420 gggggcgtat tga 3433 29 3075 DNA Aspergillus CDS (1)...(3075) 29 atg aag ctt ctc tct gtc tgc gca att gcc ttg ttg gca gct cag gca 48 Met Lys Leu Leu Ser Val Cys Ala Ile Ala Leu Leu Ala Ala Gln Ala 1 5 10 15 gcg ggt gct tcc atc aag cac atg ctc aat ggc ttc act ctt atg gag 96 Ala Gly Ala Ser Ile Lys His Met Leu Asn Gly Phe Thr Leu Met Glu 20 25 30 cac tcg gat cct gcg aag cgg gaa ctg cta cag aaa tac gtc acc tgg 144 His Ser Asp Pro Ala Lys Arg Glu Leu Leu Gln Lys Tyr Val Thr Trp 35 40 45 gat gag aag tca ctg ttt gtc aat ggc gag aga atc atg att ttc agc 192 Asp Glu Lys Ser Leu Phe Val Asn Gly Glu Arg Ile Met Ile Phe Ser 50 55 60 ggc gaa gtt cac cct ttc aga ctg ccc gtt cct tcg ctg tgg ctc gat 240 Gly Glu Val His Pro Phe Arg Leu Pro Val Pro Ser Leu Trp Leu Asp 65 70 75 80 gtc ttt cag aaa atc aag gcc ctg ggg ttc aat tgc gtt tca ttc tac 288 Val Phe Gln Lys Ile Lys Ala Leu Gly Phe Asn Cys Val Ser Phe Tyr 85 90 95 gtc gac tgg gcc ctc ctc gaa gga aaa cct ggc gag tac agg gct gaa 336 Val Asp Trp Ala Leu Leu Glu Gly Lys Pro Gly Glu Tyr Arg Ala Glu 100 105 110 ggc aac ttt gcc ctc gag cct ttc ttt gac gtg gct aag cag gca gga 384 Gly Asn Phe Ala Leu Glu Pro Phe Phe Asp Val Ala Lys Gln Ala Gly 115 120 125 atc tat ctc ctc gct cgt cct gga cct tat atc aat gct gag gct tcg 432 Ile Tyr Leu Leu Ala Arg Pro Gly Pro Tyr Ile Asn Ala Glu Ala Ser 130 135 140 ggc ggt ggt ttc cct gga tgg ttg cag aga gtg aac gga acc ctg cgg 480 Gly Gly Gly Phe Pro Gly Trp Leu Gln Arg Val Asn Gly Thr Leu Arg 145 150 155 160 aca tcc gat ccc gcg tac ctg aag gct act gat aac tac att gcc cat 528 Thr Ser Asp Pro Ala Tyr Leu Lys Ala Thr Asp Asn Tyr Ile Ala His 165 170 175 gtt gct gct act att gcc aaa ggc caa atc aca aac ggg ggc ccc gtc 576 Val Ala Ala Thr Ile Ala Lys Gly Gln Ile Thr Asn Gly Gly Pro Val 180 185 190 att ctt tat caa ccg gag aat gag tac agc ggg gcg tgt tgt gat gct 624 Ile Leu Tyr Gln Pro Glu Asn Glu Tyr Ser Gly Ala Cys Cys Asp Ala 195 200 205 act ttc ccc gat ggg gac tac atg caa tat gtc atc gac cag gct cga 672 Thr Phe Pro Asp Gly Asp Tyr Met Gln Tyr Val Ile Asp Gln Ala Arg 210 215 220 aac gcc ggt att gtt gta cca ttg atc aat aac gat gcc tgg act gga 720 Asn Ala Gly Ile Val Val Pro Leu Ile Asn Asn Asp Ala Trp Thr Gly 225 230 235 240 gga cac aat gcc cct ggg acg ggc aag ggc gag gtt gac atc tat ggt 768 Gly His Asn Ala Pro Gly Thr Gly Lys Gly Glu Val Asp Ile Tyr Gly 245 250 255 cac gat agc tat cca cta gga ttt gac tgt gga cac cca agc gtt tgg 816 His Asp Ser Tyr Pro Leu Gly Phe Asp Cys Gly His Pro Ser Val Trp 260 265 270 ccc aag ggc aac ctg cca acc act ttc cgg acg gat cac ttg aag cag 864 Pro Lys Gly Asn Leu Pro Thr Thr Phe Arg Thr Asp His Leu Lys Gln 275 280 285 agc ccg aca acc ccg tac tct ctt att gag gtg tgt gtg tgt ctc aaa 912 Ser Pro Thr Thr Pro Tyr Ser Leu Ile Glu Val Cys Val Cys Leu Lys 290 295 300 tgc cct cgg atc cgg aca cca cta atc gtc gtg cag ttc caa gca ggt 960 Cys Pro Arg Ile Arg Thr Pro Leu Ile Val Val Gln Phe Gln Ala Gly 305 310 315 320 tcc ttt gat cca tgg ggt gga ccc ggc ttt gca gca tgc gcc gcc ctc 1008 Ser Phe Asp Pro Trp Gly Gly Pro Gly Phe Ala Ala Cys Ala Ala Leu 325 330 335 gtc aat cac gag ttc gag aga gta ttc tac aag aat gac cta agc ttt 1056 Val Asn His Glu Phe Glu Arg Val Phe Tyr Lys Asn Asp Leu Ser Phe 340 345 350 gga gct gct atc ctg aac ttg tac atg acc ttt ggc ggc acg aac tgg 1104 Gly Ala Ala Ile Leu Asn Leu Tyr Met Thr Phe Gly Gly Thr Asn Trp 355 360 365 ggt aac ctt ggc cat ccc ggt gga tac aca tcc tac gat tat gga tcg 1152 Gly Asn Leu Gly His Pro Gly Gly Tyr Thr Ser Tyr Asp Tyr Gly Ser 370 375 380 ccg ctg act gaa tct cgc aat gtc act cga gag aag tac agt gag ctc 1200 Pro Leu Thr Glu Ser Arg Asn Val Thr Arg Glu Lys Tyr Ser Glu Leu 385 390 395 400 aag tta atc ggt aac ttc gtg aaa gcc tcg ccg tct tac ctt ctg gct 1248 Lys Leu Ile Gly Asn Phe Val Lys Ala Ser Pro Ser Tyr Leu Leu Ala 405 410 415 acg cct ggc aat ttg act acc tct gga tat gcc gac acc gct gat ttg 1296 Thr Pro Gly Asn Leu Thr Thr Ser Gly Tyr Ala Asp Thr Ala Asp Leu 420 425 430 acc gtg act cct ttg ctg ggc aat ggc act gga tcg tac ttt gtt gtc 1344 Thr Val Thr Pro Leu Leu Gly Asn Gly Thr Gly Ser Tyr Phe Val Val 435 440 445 aga cat acg gat tac acc agc cag gca tct acc ccg tac aaa ctc agc 1392 Arg His Thr Asp Tyr Thr Ser Gln Ala Ser Thr Pro Tyr Lys Leu Ser 450 455 460 ctc cca acc agt gct gga aga ctc aca gtt ccc cag ctc ggc ggt act 1440 Leu Pro Thr Ser Ala Gly Arg Leu Thr Val Pro Gln Leu Gly Gly Thr 465 470 475 480 ctg acg ctc aat gga cgt gat tcc aaa att cat gtt gtg gac tac aac 1488 Leu Thr Leu Asn Gly Arg Asp Ser Lys Ile His Val Val Asp Tyr Asn 485 490 495 gtc gcg ggg acc aat atc ata tac tcg act gcc gaa gtc ttc acc tgg 1536 Val Ala Gly Thr Asn Ile Ile Tyr Ser Thr Ala Glu Val Phe Thr Trp 500 505 510 aag aac ttt ggg gat agc aaa gtc ctc atc ttg tat ggt gga cct ggc 1584 Lys Asn Phe Gly Asp Ser Lys Val Leu Ile Leu Tyr Gly Gly Pro Gly 515 520 525 gag cac cat gag ctg gcg gtt tct ttc aag tcc gac gtc cag gtc gtc 1632 Glu His His Glu Leu Ala Val Ser Phe Lys Ser Asp Val Gln Val Val 530 535 540 gaa gga tct aat tca gaa ttc aag tcg aag aag gtg ggg gat gtt gct 1680 Glu Gly Ser Asn Ser Glu Phe Lys Ser Lys Lys Val Gly Asp Val Ala 545 550 555 560 gtg gtt gcc tgg gat gtg tct cca tcc cgc cgt att gtc cag att ggc 1728 Val Val Ala Trp Asp Val Ser Pro Ser Arg Arg Ile Val Gln Ile Gly 565 570 575 gac ctc aag ata ttc ctg ctg gat agg aac tct gtc tac aat tac tgg 1776 Asp Leu Lys Ile Phe Leu Leu Asp Arg Asn Ser Val Tyr Asn Tyr Trp 580 585 590 gtg cca caa ctt gac aag gac gac tcg tca acg ggc tac agc tcc gaa 1824 Val Pro Gln Leu Asp Lys Asp Asp Ser Ser Thr Gly Tyr Ser Ser Glu 595 600 605 aag act act gct tcg tcc att att gtc aag gct ggt tac ctt gtg cga 1872 Lys Thr Thr Ala Ser Ser Ile Ile Val Lys Ala Gly Tyr Leu Val Arg 610 615 620 acc gct tat act aag ggc tcc ggc ctc tat ctt act gct gac ttc aac 1920 Thr Ala Tyr Thr Lys Gly Ser Gly Leu Tyr Leu Thr Ala Asp Phe Asn 625 630 635 640 gca aca act cct gtc gaa gtg atc gga gcc ccg tca aac gtc cgg aac 1968 Ala Thr Thr Pro Val Glu Val Ile Gly Ala Pro Ser Asn Val Arg Asn 645 650 655 ctg tac atc aac ggc gag aag acc cag ttc aag acc gat aag aat ggt 2016 Leu Tyr Ile Asn Gly Glu Lys Thr Gln Phe Lys Thr Asp Lys Asn Gly 660 665 670 atc tgg tca act gag gtc aag tac agt gct cct aag atc aag ctt ccc 2064 Ile Trp Ser Thr Glu Val Lys Tyr Ser Ala Pro Lys Ile Lys Leu Pro 675 680 685 agc atg aag gat ctg gat tgg aag tat ctt gat act ctg cag gag gtt 2112 Ser Met Lys Asp Leu Asp Trp Lys Tyr Leu Asp Thr Leu Gln Glu Val 690 695 700 cag tca acc tat gac gat tct gcg tgg cca gca gcc gac ctg gac acc 2160 Gln Ser Thr Tyr Asp Asp Ser Ala Trp Pro Ala Ala Asp Leu Asp Thr 705 710 715 720 aca cct aac acc ttg cga ccc ttg acc acg cca aag tct ctg tac tcg 2208 Thr Pro Asn Thr Leu Arg Pro Leu Thr Thr Pro Lys Ser Leu Tyr Ser 725 730 735 tcg gac tat ggc ttc cat acg ggt tac ctg atc tac cgc ggc cac ttt 2256 Ser Asp Tyr Gly Phe His Thr Gly Tyr Leu Ile Tyr Arg Gly His Phe 740 745 750 gtt gct gac ggc agc gag act aca ttt gac gtg cgc acg caa gga ggc 2304 Val Ala Asp Gly Ser Glu Thr Thr Phe Asp Val Arg Thr Gln Gly Gly 755 760 765 tcg gcc ttt ggc agt tcc gtc tgg ctg aac gaa tca ttc cta ggc tcc 2352 Ser Ala Phe Gly Ser Ser Val Trp Leu Asn Glu Ser Phe Leu Gly Ser 770 775 780 tgg act ggt ctc aac gcc aat gcg gac tac aac tca acc tac aaa ttg 2400 Trp Thr Gly Leu Asn Ala Asn Ala Asp Tyr Asn Ser Thr Tyr Lys Leu 785 790 795 800 ccg cag gtc gag caa ggc aag aac tat gtc ctc act att ctc att gac 2448 Pro Gln Val Glu Gln Gly Lys Asn Tyr Val Leu Thr Ile Leu Ile Asp 805 810 815 aca atg ggc ctc aac gag aac tgg gtt gtc ggc acg gac gag atg aag 2496 Thr Met Gly Leu Asn Glu Asn Trp Val Val Gly Thr Asp Glu Met Lys 820 825 830 aac ccc cgg ggt att ctc tcc tac aag ctc tcc ggc cgg gac gcc tcc 2544 Asn Pro Arg Gly Ile Leu Ser Tyr Lys Leu Ser Gly Arg Asp Ala Ser 835 840 845 gcc atc acc tgg aaa ttg acc gga aac ctc ggc gga gag gat tac caa 2592 Ala Ile Thr Trp Lys Leu Thr Gly Asn Leu Gly Gly Glu Asp Tyr Gln 850 855 860 gac aag atc cgc ggc cct ctg aac gaa ggt gga ttg tat gcc gaa cgg 2640 Asp Lys Ile Arg Gly Pro Leu Asn Glu Gly Gly Leu Tyr Ala Glu Arg 865 870 875 880 caa ggc ttc cac cag ccc cag ccg ccc agc cag aag tgg aaa tca gct 2688 Gln Gly Phe His Gln Pro Gln Pro Pro Ser Gln Lys Trp Lys Ser Ala 885 890 895 agt cct ctc gat ggg tta tcc aag cct ggc att ggc ttc tac acc gct 2736 Ser Pro Leu Asp Gly Leu Ser Lys Pro Gly Ile Gly Phe Tyr Thr Ala 900 905 910 cag ttt gat ctg gat atc cca agc ggg tgg gac gtg ccg ctc tac ttc 2784 Gln Phe Asp Leu Asp Ile Pro Ser Gly Trp Asp Val Pro Leu Tyr Phe 915 920 925 aac ttt ggc aac agc acg aag tca gcc tac cgg gtg cag ctg tat gtc 2832 Asn Phe Gly Asn Ser Thr Lys Ser Ala Tyr Arg Val Gln Leu Tyr Val 930 935 940 aac gga tac cag tac ggc aag ttc gtc agc aac ata ggc cct cag aca 2880 Asn Gly Tyr Gln Tyr Gly Lys Phe Val Ser Asn Ile Gly Pro Gln Thr 945 950 955 960 agc ttc ccc gtc ccg cag ggt atc ctg aac tat cag gga acc aat tgg 2928 Ser Phe Pro Val Pro Gln Gly Ile Leu Asn Tyr Gln Gly Thr Asn Trp 965 970 975 gtt gcg ttg act ctc tgg gca ctc gag tcg gat ggt gcc aag ttg gat 2976 Val Ala Leu Thr Leu Trp Ala Leu Glu Ser Asp Gly Ala Lys Leu Asp 980 985 990 gac ttt gag ttg gtg aac acc aca cca gtc atg act gcc cta tca aaa 3024 Asp Phe Glu Leu Val Asn Thr Thr Pro Val Met Thr Ala Leu Ser Lys 995 1000 1005 att cgg cca tca aag cag cca aat tat cgt caa cgg aag ggg gcg tat 3072 Ile Arg Pro Ser Lys Gln Pro Asn Tyr Arg Gln Arg Lys Gly Ala Tyr 1010 1015 1020 tga 3075 * 30 1024 PRT Aspergillus 30 Met Lys Leu Leu Ser Val Cys Ala Ile Ala Leu Leu Ala Ala Gln Ala 1 5 10 15 Ala Gly Ala Ser Ile Lys His Met Leu Asn Gly Phe Thr Leu Met Glu 20 25 30 His Ser Asp Pro Ala Lys Arg Glu Leu Leu Gln Lys Tyr Val Thr Trp 35 40 45 Asp Glu Lys Ser Leu Phe Val Asn Gly Glu Arg Ile Met Ile Phe Ser 50 55 60 Gly Glu Val His Pro Phe Arg Leu Pro Val Pro Ser Leu Trp Leu Asp 65 70 75 80 Val Phe Gln Lys Ile Lys Ala Leu Gly Phe Asn Cys Val Ser Phe Tyr 85 90 95 Val Asp Trp Ala Leu Leu Glu Gly Lys Pro Gly Glu Tyr Arg Ala Glu 100 105 110 Gly Asn Phe Ala Leu Glu Pro Phe Phe Asp Val Ala Lys Gln Ala Gly 115 120 125 Ile Tyr Leu Leu Ala Arg Pro Gly Pro Tyr Ile Asn Ala Glu Ala Ser 130 135 140 Gly Gly Gly Phe Pro Gly Trp Leu Gln Arg Val Asn Gly Thr Leu Arg 145 150 155 160 Thr Ser Asp Pro Ala Tyr Leu Lys Ala Thr Asp Asn Tyr Ile Ala His 165 170 175 Val Ala Ala Thr Ile Ala Lys Gly Gln Ile Thr Asn Gly Gly Pro Val 180 185 190 Ile Leu Tyr Gln Pro Glu Asn Glu Tyr Ser Gly Ala Cys Cys Asp Ala 195 200 205 Thr Phe Pro Asp Gly Asp Tyr Met Gln Tyr Val Ile Asp Gln Ala Arg 210 215 220 Asn Ala Gly Ile Val Val Pro Leu Ile Asn Asn Asp Ala Trp Thr Gly 225 230 235 240 Gly His Asn Ala Pro Gly Thr Gly Lys Gly Glu Val Asp Ile Tyr Gly 245 250 255 His Asp Ser Tyr Pro Leu Gly Phe Asp Cys Gly His Pro Ser Val Trp 260 265 270 Pro Lys Gly Asn Leu Pro Thr Thr Phe Arg Thr Asp His Leu Lys Gln 275 280 285 Ser Pro Thr Thr Pro Tyr Ser Leu Ile Glu Val Cys Val Cys Leu Lys 290 295 300 Cys Pro Arg Ile Arg Thr Pro Leu Ile Val Val Gln Phe Gln Ala Gly 305 310 315 320 Ser Phe Asp Pro Trp Gly Gly Pro Gly Phe Ala Ala Cys Ala Ala Leu 325 330 335 Val Asn His Glu Phe Glu Arg Val Phe Tyr Lys Asn Asp Leu Ser Phe 340 345 350 Gly Ala Ala Ile Leu Asn Leu Tyr Met Thr Phe Gly Gly Thr Asn Trp 355 360 365 Gly Asn Leu Gly His Pro Gly Gly Tyr Thr Ser Tyr Asp Tyr Gly Ser 370 375 380 Pro Leu Thr Glu Ser Arg Asn Val Thr Arg Glu Lys Tyr Ser Glu Leu 385 390 395 400 Lys Leu Ile Gly Asn Phe Val Lys Ala Ser Pro Ser Tyr Leu Leu Ala 405 410 415 Thr Pro Gly Asn Leu Thr Thr Ser Gly Tyr Ala Asp Thr Ala Asp Leu 420 425 430 Thr Val Thr Pro Leu Leu Gly Asn Gly Thr Gly Ser Tyr Phe Val Val 435 440 445 Arg His Thr Asp Tyr Thr Ser Gln Ala Ser Thr Pro Tyr Lys Leu Ser 450 455 460 Leu Pro Thr Ser Ala Gly Arg Leu Thr Val Pro Gln Leu Gly Gly Thr 465 470 475 480 Leu Thr Leu Asn Gly Arg Asp Ser Lys Ile His Val Val Asp Tyr Asn 485 490 495 Val Ala Gly Thr Asn Ile Ile Tyr Ser Thr Ala Glu Val Phe Thr Trp 500 505 510 Lys Asn Phe Gly Asp Ser Lys Val Leu Ile Leu Tyr Gly Gly Pro Gly 515 520 525 Glu His His Glu Leu Ala Val Ser Phe Lys Ser Asp Val Gln Val Val 530 535 540 Glu Gly Ser Asn Ser Glu Phe Lys Ser Lys Lys Val Gly Asp Val Ala 545 550 555 560 Val Val Ala Trp Asp Val Ser Pro Ser Arg Arg Ile Val Gln Ile Gly 565 570 575 Asp Leu Lys Ile Phe Leu Leu Asp Arg Asn Ser Val Tyr Asn Tyr Trp 580 585 590 Val Pro Gln Leu Asp Lys Asp Asp Ser Ser Thr Gly Tyr Ser Ser Glu 595 600 605 Lys Thr Thr Ala Ser Ser Ile Ile Val Lys Ala Gly Tyr Leu Val Arg 610 615 620 Thr Ala Tyr Thr Lys Gly Ser Gly Leu Tyr Leu Thr Ala Asp Phe Asn 625 630 635 640 Ala Thr Thr Pro Val Glu Val Ile Gly Ala Pro Ser Asn Val Arg Asn 645 650 655 Leu Tyr Ile Asn Gly Glu Lys Thr Gln Phe Lys Thr Asp Lys Asn Gly 660 665 670 Ile Trp Ser Thr Glu Val Lys Tyr Ser Ala Pro Lys Ile Lys Leu Pro 675 680 685 Ser Met Lys Asp Leu Asp Trp Lys Tyr Leu Asp Thr Leu Gln Glu Val 690 695 700 Gln Ser Thr Tyr Asp Asp Ser Ala Trp Pro Ala Ala Asp Leu Asp Thr 705 710 715 720 Thr Pro Asn Thr Leu Arg Pro Leu Thr Thr Pro Lys Ser Leu Tyr Ser 725 730 735 Ser Asp Tyr Gly Phe His Thr Gly Tyr Leu Ile Tyr Arg Gly His Phe 740 745 750 Val Ala Asp Gly Ser Glu Thr Thr Phe Asp Val Arg Thr Gln Gly Gly 755 760 765 Ser Ala Phe Gly Ser Ser Val Trp Leu Asn Glu Ser Phe Leu Gly Ser 770 775 780 Trp Thr Gly Leu Asn Ala Asn Ala Asp Tyr Asn Ser Thr Tyr Lys Leu 785 790 795 800 Pro Gln Val Glu Gln Gly Lys Asn Tyr Val Leu Thr Ile Leu Ile Asp 805 810 815 Thr Met Gly Leu Asn Glu Asn Trp Val Val Gly Thr Asp Glu Met Lys 820 825 830 Asn Pro Arg Gly Ile Leu Ser Tyr Lys Leu Ser Gly Arg Asp Ala Ser 835 840 845 Ala Ile Thr Trp Lys Leu Thr Gly Asn Leu Gly Gly Glu Asp Tyr Gln 850 855 860 Asp Lys Ile Arg Gly Pro Leu Asn Glu Gly Gly Leu Tyr Ala Glu Arg 865 870 875 880 Gln Gly Phe His Gln Pro Gln Pro Pro Ser Gln Lys Trp Lys Ser Ala 885 890 895 Ser Pro Leu Asp Gly Leu Ser Lys Pro Gly Ile Gly Phe Tyr Thr Ala 900 905 910 Gln Phe Asp Leu Asp Ile Pro Ser Gly Trp Asp Val Pro Leu Tyr Phe 915 920 925 Asn Phe Gly Asn Ser Thr Lys Ser Ala Tyr Arg Val Gln Leu Tyr Val 930 935 940 Asn Gly Tyr Gln Tyr Gly Lys Phe Val Ser Asn Ile Gly Pro Gln Thr 945 950 955 960 Ser Phe Pro Val Pro Gln Gly Ile Leu Asn Tyr Gln Gly Thr Asn Trp 965 970 975 Val Ala Leu Thr Leu Trp Ala Leu Glu Ser Asp Gly Ala Lys Leu Asp 980 985 990 Asp Phe Glu Leu Val Asn Thr Thr Pro Val Met Thr Ala Leu Ser Lys 995 1000 1005 Ile Arg Pro Ser Lys Gln Pro Asn Tyr Arg Gln Arg Lys Gly Ala Tyr 1010 1015 1020 31 1977 DNA Aspergillus 31 atgcgatttg ctggcattgc tgtaggcata gccagtgtcc tagggcactt ggccactcct 60 tcgtctgcta aagaacttgc tgcacgctcc cctgcagcgg caaattcacg tctggtcaaa 120 gagggactgt tcgcctacga gagcattctt gcggctcttg ggaacactgg catcaatgct 180 cctggcacag cggctggatt actcattgca agtcctacca tacagaaccc tgattgtagg 240 tgaaaaaggc cccgttagga agatcaagtt gacttgatct gctccattct ctagacttct 300 atacgtggac tcgggatgcg gcattgactt tcaaaggact tgtcgatatc ttcattgggg 360 gcgatacatt tatcgtcgtc aatctcgacg gtcttgaaac ccacatccag gactacatct 420 cttcccaggc agttttgcag aacgtgtcca acccatccgg aagactttct gacggctctg 480 gactcggcga gcccaagttc gaggtcaatt tcaacccata ctccggcggt tggggccgtc 540 cccagcgcga tggtcctgcc cttcgcgcca ttaccatgtt gacctatatt cgtcagctaa 600 tccagcaagg gaaacagtct gtggcttcca acctgatctg gcccgttgta gccaacgatc 660 tcacctatgt cgcgcagtac tggaaccaca ccggattcga tctctgggaa gaaatcgatg 720 gctcttcctt ctttacgact gccgtgcagc accgagcgat ggttgagggt agtgcgatag 780 ctcaagccct tggtaagcca catgctgggt atgacgcggt tgctcccgag attctttgct 840 tgctgcagag ctactggaac gaaagcgcca ttatctcgaa catcaatgtc aataacggcc 900 ggtcgggcat cgatctcaac tcagtcctga ccagtattca tacctttgac cctgcggctg 960 gttgtgatga ttccaccttc caacaatgtt cgtctaaggc tttggcaaat cataaggtct 1020 atgtcgattc tttccgttct atctacggta tcaacgctgg ccttggtcct ggaaaggctg 1080 caaatgtagg ccgttacgct gaagatattt accagggagg aaacccatgg taggtcaaac 1140 caatctcctc acttactacg tgtcagactt ctgatggatt aaaggtacct cgcaactctt 1200 gcggcggcag agcagctgta tgatgccctc tatcagtgga aaaagcaggg ttatctgacc 1260 gtcacacaaa cctcgctcgc cttcttccgt gacttctcgt ccaccgtcga gccaggaact 1320 tacaagtcga ataccccgaa ctacaaatcc ctgactgagt atgtccgcac ctacgctgat 1380 gacttcttct tccttgttga gaaatacacc ccaagcaacg gctccttagc cgagcagtat 1440 gaccgcaaca ccggtgtccc tctgtcagcc aacgatctta cctggtccta tgcagccttc 1500 ctctctaccc ttcagcgccg cctcaacatc atgcctgact cctggggccc ctcgtctgca 1560 aatactgttc ccactacctg cagcaaaacc accataactg gtacatacag tgctgtggcg 1620 cctccctttc cgacgtccac cgctcagtgc gttgccgctg tgactgttcc tgtcaccttt 1680 tggttgatcg agaataccta ctatggcgag aatgtgtaca tgaccggcaa cgtcagcgct 1740 ctcggcgact ggaacgccag cgcaggctat agtctgaatg ccggtctcta cacctcggat 1800 gagaatcttt ggttcgcaac tgtcaaggga ctcgagccgg gtgttaccat ggagtacaag 1860 ttctacaaga ttgaaccggg aaactccgtg acttttgagg ggggggagaa cagggtgtat 1920 gcagttccta cagcatgtcc tgtggcgcct caggtccacg ctgtttggca gacctga 1977 32 1863 DNA Aspergillus CDS (1)...(1863) 32 atg cga ttt gct ggc att gct gta ggc ata gcc agt gtc cta ggg cac 48 Met Arg Phe Ala Gly Ile Ala Val Gly Ile Ala Ser Val Leu Gly His 1 5 10 15 ttg gcc act cct tcg tct gct aaa gaa ctt gct gca cgc tcc cct gca 96 Leu Ala Thr Pro Ser Ser Ala Lys Glu Leu Ala Ala Arg Ser Pro Ala 20 25 30 gcg gca aat tca cgt ctg gtc aaa gag gga ctg ttc gcc tac gag agc 144 Ala Ala Asn Ser Arg Leu Val Lys Glu Gly Leu Phe Ala Tyr Glu Ser 35 40 45 att ctt gcg gct ctt ggg aac act ggc atc aat gct cct ggc aca gcg 192 Ile Leu Ala Ala Leu Gly Asn Thr Gly Ile Asn Ala Pro Gly Thr Ala 50 55 60 gct gga tta ctc att gca agt cct acc ata cag aac cct gat tac ttc 240 Ala Gly Leu Leu Ile Ala Ser Pro Thr Ile Gln Asn Pro Asp Tyr Phe 65 70 75 80 tat acg tgg act cgg gat gcg gca ttg act ttc aaa gga ctt gtc gat 288 Tyr Thr Trp Thr Arg Asp Ala Ala Leu Thr Phe Lys Gly Leu Val Asp 85 90 95 atc ttc att ggg ggc gat aca ttt atc gtc gtc aat ctc gac ggt ctt 336 Ile Phe Ile Gly Gly Asp Thr Phe Ile Val Val Asn Leu Asp Gly Leu 100 105 110 gaa acc cac atc cag gac tac atc tct tcc cag gca gtt ttg cag aac 384 Glu Thr His Ile Gln Asp Tyr Ile Ser Ser Gln Ala Val Leu Gln Asn 115 120 125 gtg tcc aac cca tcc gga aga ctt tct gac ggc tct gga ctc ggc gag 432 Val Ser Asn Pro Ser Gly Arg Leu Ser Asp Gly Ser Gly Leu Gly Glu 130 135 140 ccc aag ttc gag gtc aat ttc aac cca tac tcc ggc ggt tgg ggc cgt 480 Pro Lys Phe Glu Val Asn Phe Asn Pro Tyr Ser Gly Gly Trp Gly Arg 145 150 155 160 ccc cag cgc gat ggt cct gcc ctt cgc gcc att acc atg ttg acc tat 528 Pro Gln Arg Asp Gly Pro Ala Leu Arg Ala Ile Thr Met Leu Thr Tyr 165 170 175 att cgt cag cta atc cag caa ggg aaa cag tct gtg gct tcc aac ctg 576 Ile Arg Gln Leu Ile Gln Gln Gly Lys Gln Ser Val Ala Ser Asn Leu 180 185 190 atc tgg ccc gtt gta gcc aac gat ctc acc tat gtc gcg cag tac tgg 624 Ile Trp Pro Val Val Ala Asn Asp Leu Thr Tyr Val Ala Gln Tyr Trp 195 200 205 aac cac acc gga ttc gat ctc tgg gaa gaa atc gat ggc tct tcc ttc 672 Asn His Thr Gly Phe Asp Leu Trp Glu Glu Ile Asp Gly Ser Ser Phe 210 215 220 ttt acg act gcc gtg cag cac cga gcg atg gtt gag ggt agt gcg ata 720 Phe Thr Thr Ala Val Gln His Arg Ala Met Val Glu Gly Ser Ala Ile 225 230 235 240 gct caa gcc ctt ggt aag cca cat gct ggg tat gac gcg gtt gct ccc 768 Ala Gln Ala Leu Gly Lys Pro His Ala Gly Tyr Asp Ala Val Ala Pro 245 250 255 gag att ctt tgc ttg ctg cag agc tac tgg aac gaa agc gcc att atc 816 Glu Ile Leu Cys Leu Leu Gln Ser Tyr Trp Asn Glu Ser Ala Ile Ile 260 265 270 tcg aac atc aat gtc aat aac ggc cgg tcg ggc atc gat ctc aac tca 864 Ser Asn Ile Asn Val Asn Asn Gly Arg Ser Gly Ile Asp Leu Asn Ser 275 280 285 gtc ctg acc agt att cat acc ttt gac cct gcg gct ggt tgt gat gat 912 Val Leu Thr Ser Ile His Thr Phe Asp Pro Ala Ala Gly Cys Asp Asp 290 295 300 tcc acc ttc caa caa tgt tcg tct aag gct ttg gca aat cat aag gtc 960 Ser Thr Phe Gln Gln Cys Ser Ser Lys Ala Leu Ala Asn His Lys Val 305 310 315 320 tat gtc gat tct ttc cgt tct atc tac ggt atc aac gct ggc ctt ggt 1008 Tyr Val Asp Ser Phe Arg Ser Ile Tyr Gly Ile Asn Ala Gly Leu Gly 325 330 335 cct gga aag gct gca aat gta ggc cgt tac gct gaa gat att tac cag 1056 Pro Gly Lys Ala Ala Asn Val Gly Arg Tyr Ala Glu Asp Ile Tyr Gln 340 345 350 gga gga aac cca tgg tac ctc gca act ctt gcg gcg gca gag cag ctg 1104 Gly Gly Asn Pro Trp Tyr Leu Ala Thr Leu Ala Ala Ala Glu Gln Leu 355 360 365 tat gat gcc ctc tat cag tgg aaa aag cag ggt tat ctg acc gtc aca 1152 Tyr Asp Ala Leu Tyr Gln Trp Lys Lys Gln Gly Tyr Leu Thr Val Thr 370 375 380 caa acc tcg ctc gcc ttc ttc cgt gac ttc tcg tcc acc gtc gag cca 1200 Gln Thr Ser Leu Ala Phe Phe Arg Asp Phe Ser Ser Thr Val Glu Pro 385 390 395 400 gga act tac aag tcg aat acc ccg aac tac aaa tcc ctg act gag tat 1248 Gly Thr Tyr Lys Ser Asn Thr Pro Asn Tyr Lys Ser Leu Thr Glu Tyr 405 410 415 gtc cgc acc tac gct gat gac ttc ttc ttc ctt gtt gag aaa tac acc 1296 Val Arg Thr Tyr Ala Asp Asp Phe Phe Phe Leu Val Glu Lys Tyr Thr 420 425 430 cca agc aac ggc tcc tta gcc gag cag tat gac cgc aac acc ggt gtc 1344 Pro Ser Asn Gly Ser Leu Ala Glu Gln Tyr Asp Arg Asn Thr Gly Val 435 440 445 cct ctg tca gcc aac gat ctt acc tgg tcc tat gca gcc ttc ctc tct 1392 Pro Leu Ser Ala Asn Asp Leu Thr Trp Ser Tyr Ala Ala Phe Leu Ser 450 455 460 acc ctt cag cgc cgc ctc aac atc atg cct gac tcc tgg ggc ccc tcg 1440 Thr Leu Gln Arg Arg Leu Asn Ile Met Pro Asp Ser Trp Gly Pro Ser 465 470 475 480 tct gca aat act gtt ccc act acc tgc agc aaa acc acc ata act ggt 1488 Ser Ala Asn Thr Val Pro Thr Thr Cys Ser Lys Thr Thr Ile Thr Gly 485 490 495 aca tac agt gct gtg gcg cct ccc ttt ccg acg tcc acc gct cag tgc 1536 Thr Tyr Ser Ala Val Ala Pro Pro Phe Pro Thr Ser Thr Ala Gln Cys 500 505 510 gtt gcc gct gtg act gtt cct gtc acc ttt tgg ttg atc gag aat acc 1584 Val Ala Ala Val Thr Val Pro Val Thr Phe Trp Leu Ile Glu Asn Thr 515 520 525 tac tat ggc gag aat gtg tac atg acc ggc aac gtc agc gct ctc ggc 1632 Tyr Tyr Gly Glu Asn Val Tyr Met Thr Gly Asn Val Ser Ala Leu Gly 530 535 540 gac tgg aac gcc agc gca ggc tat agt ctg aat gcc ggt ctc tac acc 1680 Asp Trp Asn Ala Ser Ala Gly Tyr Ser Leu Asn Ala Gly Leu Tyr Thr 545 550 555 560 tcg gat gag aat ctt tgg ttc gca act gtc aag gga ctc gag ccg ggt 1728 Ser Asp Glu Asn Leu Trp Phe Ala Thr Val Lys Gly Leu Glu Pro Gly 565 570 575 gtt acc atg gag tac aag ttc tac aag att gaa ccg gga aac tcc gtg 1776 Val Thr Met Glu Tyr Lys Phe Tyr Lys Ile Glu Pro Gly Asn Ser Val 580 585 590 act ttt gag ggg ggg gag aac agg gtg tat gca gtt cct aca gca tgt 1824 Thr Phe Glu Gly Gly Glu Asn Arg Val Tyr Ala Val Pro Thr Ala Cys 595 600 605 cct gtg gcg cct cag gtc cac gct gtt tgg cag acc tga 1863 Pro Val Ala Pro Gln Val His Ala Val Trp Gln Thr * 610 615 620 33 620 PRT Aspergillus 33 Met Arg Phe Ala Gly Ile Ala Val Gly Ile Ala Ser Val Leu Gly His 1 5 10 15 Leu Ala Thr Pro Ser Ser Ala Lys Glu Leu Ala Ala Arg Ser Pro Ala 20 25 30 Ala Ala Asn Ser Arg Leu Val Lys Glu Gly Leu Phe Ala Tyr Glu Ser 35 40 45 Ile Leu Ala Ala Leu Gly Asn Thr Gly Ile Asn Ala Pro Gly Thr Ala 50 55 60 Ala Gly Leu Leu Ile Ala Ser Pro Thr Ile Gln Asn Pro Asp Tyr Phe 65 70 75 80 Tyr Thr Trp Thr Arg Asp Ala Ala Leu Thr Phe Lys Gly Leu Val Asp 85 90 95 Ile Phe Ile Gly Gly Asp Thr Phe Ile Val Val Asn Leu Asp Gly Leu 100 105 110 Glu Thr His Ile Gln Asp Tyr Ile Ser Ser Gln Ala Val Leu Gln Asn 115 120 125 Val Ser Asn Pro Ser Gly Arg Leu Ser Asp Gly Ser Gly Leu Gly Glu 130 135 140 Pro Lys Phe Glu Val Asn Phe Asn Pro Tyr Ser Gly Gly Trp Gly Arg 145 150 155 160 Pro Gln Arg Asp Gly Pro Ala Leu Arg Ala Ile Thr Met Leu Thr Tyr 165 170 175 Ile Arg Gln Leu Ile Gln Gln Gly Lys Gln Ser Val Ala Ser Asn Leu 180 185 190 Ile Trp Pro Val Val Ala Asn Asp Leu Thr Tyr Val Ala Gln Tyr Trp 195 200 205 Asn His Thr Gly Phe Asp Leu Trp Glu Glu Ile Asp Gly Ser Ser Phe 210 215 220 Phe Thr Thr Ala Val Gln His Arg Ala Met Val Glu Gly Ser Ala Ile 225 230 235 240 Ala Gln Ala Leu Gly Lys Pro His Ala Gly Tyr Asp Ala Val Ala Pro 245 250 255 Glu Ile Leu Cys Leu Leu Gln Ser Tyr Trp Asn Glu Ser Ala Ile Ile 260 265 270 Ser Asn Ile Asn Val Asn Asn Gly Arg Ser Gly Ile Asp Leu Asn Ser 275 280 285 Val Leu Thr Ser Ile His Thr Phe Asp Pro Ala Ala Gly Cys Asp Asp 290 295 300 Ser Thr Phe Gln Gln Cys Ser Ser Lys Ala Leu Ala Asn His Lys Val 305 310 315 320 Tyr Val Asp Ser Phe Arg Ser Ile Tyr Gly Ile Asn Ala Gly Leu Gly 325 330 335 Pro Gly Lys Ala Ala Asn Val Gly Arg Tyr Ala Glu Asp Ile Tyr Gln 340 345 350 Gly Gly Asn Pro Trp Tyr Leu Ala Thr Leu Ala Ala Ala Glu Gln Leu 355 360 365 Tyr Asp Ala Leu Tyr Gln Trp Lys Lys Gln Gly Tyr Leu Thr Val Thr 370 375 380 Gln Thr Ser Leu Ala Phe Phe Arg Asp Phe Ser Ser Thr Val Glu Pro 385 390 395 400 Gly Thr Tyr Lys Ser Asn Thr Pro Asn Tyr Lys Ser Leu Thr Glu Tyr 405 410 415 Val Arg Thr Tyr Ala Asp Asp Phe Phe Phe Leu Val Glu Lys Tyr Thr 420 425 430 Pro Ser Asn Gly Ser Leu Ala Glu Gln Tyr Asp Arg Asn Thr Gly Val 435 440 445 Pro Leu Ser Ala Asn Asp Leu Thr Trp Ser Tyr Ala Ala Phe Leu Ser 450 455 460 Thr Leu Gln Arg Arg Leu Asn Ile Met Pro Asp Ser Trp Gly Pro Ser 465 470 475 480 Ser Ala Asn Thr Val Pro Thr Thr Cys Ser Lys Thr Thr Ile Thr Gly 485 490 495 Thr Tyr Ser Ala Val Ala Pro Pro Phe Pro Thr Ser Thr Ala Gln Cys 500 505 510 Val Ala Ala Val Thr Val Pro Val Thr Phe Trp Leu Ile Glu Asn Thr 515 520 525 Tyr Tyr Gly Glu Asn Val Tyr Met Thr Gly Asn Val Ser Ala Leu Gly 530 535 540 Asp Trp Asn Ala Ser Ala Gly Tyr Ser Leu Asn Ala Gly Leu Tyr Thr 545 550 555 560 Ser Asp Glu Asn Leu Trp Phe Ala Thr Val Lys Gly Leu Glu Pro Gly 565 570 575 Val Thr Met Glu Tyr Lys Phe Tyr Lys Ile Glu Pro Gly Asn Ser Val 580 585 590 Thr Phe Glu Gly Gly Glu Asn Arg Val Tyr Ala Val Pro Thr Ala Cys 595 600 605 Pro Val Ala Pro Gln Val His Ala Val Trp Gln Thr 610 615 620 34 1943 DNA Aspergillus 34 atgcatatcc ttccaggatc ccaacatgcg gcagagttgg acaacagtgg aactctaata 60 cactctgtcc attgcgatcc agaacagaaa gccaagaata tcccgcaatc gacgggtata 120 gctcaagcga gctctgaatg gcgaccgtca taccatcttg ctgcgccccg ggggtggatg 180 aatgacccct gtgggcttgg gtatgacccg acgactggac tgtaccacct gtccttccaa 240 tggaacccgc atgggaatga ctggggcaac atctcctggg gccatgccac ctccagcgat 300 ctagtgtcct ggcaaatatc ccccgaacca tgtctcacgc cgtctgcgga gtatgatcga 360 tgcggcgtgt tcactggctg cttccgttct catggtccag atggcaagcc aggtgtacta 420 acgtatgtat acacatccgt aaatcacctt ccactccact atactctgcc gtatgtcaag 480 ggcagtgaat cgctcagtat agctgtctcc cgtgaccatg gcaagacctg gcaacgaatc 540 gacagtaatc cgattcaccc cggcgcccct gcaggactcg aggtgacagg ctggagagac 600 ccttatctga actgctggcc ctcgttgcgg gcccagcgac agggtggagt ggcctccccg 660 gatctgtatg gatttatctc cgggggcatc gctaaagagt ccccaacagt ctttgtatat 720 gtcgtcaatc ccgacaatct gactgagtgg acatatatcg ggcctttgct tcatgttggc 780 ttgaattatc gaccctctcg atggtcgggg gatctcggcg tcaactggga agttgccaac 840 ttctttacgt tgacagatgg cggcgtctcc cgggatatcg tgatcttcgg cgcagaggga 900 tgcttgtctt gcgaggttgg atcaaagaga gtaccgcgct ctttgctctg gatgtgcatt 960 aatgtccgac ctggactgca ggcgcaaagc agtggcgagc ctctcgcaga ttattcattc 1020 tcggggatct tcgatcacgg gtgctgctac gctgcaaact ctttctggga cccggtcacg 1080 gaggagtatg tcgtatactg ctggattaca gaggaggatt taccagatcg cctgcgccat 1140 cgacaaggct ggagtggcat catgtctcta ccgcgactag taaggctggt gactcttcac 1200 aatgtcaagc gagcccacca gtcaaagctg gaatccatta cgtctgtcga aatagagcgc 1260 cattcgcaag gtactcaggt ccgaaccttg agtgtccggc ctgaccccag gctcaacata 1320 cttcgaacat cggctcgaga gctgcattta tccaatgtac aactgggctc tgtggcccat 1380 cagcccccgg cattcttgcc cctgcgcact gctaggtggg aaatgaccgc gactttcgtg 1440 attgggacgc attgcgcggc agtaggattg gaaatcggcc atagccctgg tgagctctca 1500 cgcttcttct tttcccaaaa ttgcaacaaa tgctgacgca caaagaagat ttccaccagc 1560 gcaccaccct atcatggata ccatacgacg agacgttcac aatcgaacgg cctccgcttc 1620 acgatgccgg tatcaaccat gtccccgaga ccgctccgca tactctcttc accttctgca 1680 acaatgaagg cgaggaggtg acggaaccgc ttcagatcca cgcctatttc gatgcaagtg 1740 tgctagaagt gtttgtgaat agcaggacag tcatctccac acgcatctat acaccccacg 1800 cgcaggtctg cacggggctg aaattcttcg cctcggcaac cgaaagtcag ccgaaaccat 1860 caacatctgc tcctgctgct gtgctggtga gagcagatat ttgggatgga ctgagtgtga 1920 ttcgtgatga aattaagcat tag 1943 35 1887 DNA Aspergillus CDS (1)...(1887) 35 atg cat atc ctt cca gga tcc caa cat gcg gca gag ttg gac aac agt 48 Met His Ile Leu Pro Gly Ser Gln His Ala Ala Glu Leu Asp Asn Ser 1 5 10 15 gga act cta ata cac tct gtc cat tgc gat cca gaa cag aaa gcc aag 96 Gly Thr Leu Ile His Ser Val His Cys Asp Pro Glu Gln Lys Ala Lys 20 25 30 aat atc ccg caa tcg acg ggt ata gct caa gcg agc tct gaa tgg cga 144 Asn Ile Pro Gln Ser Thr Gly Ile Ala Gln Ala Ser Ser Glu Trp Arg 35 40 45 ccg tca tac cat ctt gct gcg ccc cgg ggg tgg atg aat gac ccc tgt 192 Pro Ser Tyr His Leu Ala Ala Pro Arg Gly Trp Met Asn Asp Pro Cys 50 55 60 ggg ctt ggg tat gac ccg acg act gga ctg tac cac ctg tcc ttc caa 240 Gly Leu Gly Tyr Asp Pro Thr Thr Gly Leu Tyr His Leu Ser Phe Gln 65 70 75 80 tgg aac ccg cat ggg aat gac tgg ggc aac atc tcc tgg ggc cat gcc 288 Trp Asn Pro His Gly Asn Asp Trp Gly Asn Ile Ser Trp Gly His Ala 85 90 95 acc tcc agc gat cta gtg tcc tgg caa ata tcc ccc gaa cca tgt ctc 336 Thr Ser Ser Asp Leu Val Ser Trp Gln Ile Ser Pro Glu Pro Cys Leu 100 105 110 acg ccg tct gcg gag tat gat cga tgc ggc gtg ttc act ggc tgc ttc 384 Thr Pro Ser Ala Glu Tyr Asp Arg Cys Gly Val Phe Thr Gly Cys Phe 115 120 125 cgt tct cat ggt cca gat ggc aag cca ggt gta cta acg tat gta tac 432 Arg Ser His Gly Pro Asp Gly Lys Pro Gly Val Leu Thr Tyr Val Tyr 130 135 140 aca tcc gta aat cac ctt cca ctc cac tat act ctg ccg tat gtc aag 480 Thr Ser Val Asn His Leu Pro Leu His Tyr Thr Leu Pro Tyr Val Lys 145 150 155 160 ggc agt gaa tcg ctc agt ata gct gtc tcc cgt gac cat ggc aag acc 528 Gly Ser Glu Ser Leu Ser Ile Ala Val Ser Arg Asp His Gly Lys Thr 165 170 175 tgg caa cga atc gac agt aat ccg att cac ccc ggc gcc cct gca gga 576 Trp Gln Arg Ile Asp Ser Asn Pro Ile His Pro Gly Ala Pro Ala Gly 180 185 190 ctc gag gtg aca ggc tgg aga gac cct tat ctg aac tgc tgg ccc tcg 624 Leu Glu Val Thr Gly Trp Arg Asp Pro Tyr Leu Asn Cys Trp Pro Ser 195 200 205 ttg cgg gcc cag cga cag ggt gga gtg gcc tcc ccg gat ctg tat gga 672 Leu Arg Ala Gln Arg Gln Gly Gly Val Ala Ser Pro Asp Leu Tyr Gly 210 215 220 ttt atc tcc ggg ggc atc gct aaa gag tcc cca aca gtc ttt gta tat 720 Phe Ile Ser Gly Gly Ile Ala Lys Glu Ser Pro Thr Val Phe Val Tyr 225 230 235 240 gtc gtc aat ccc gac aat ctg act gag tgg aca tat atc ggg cct ttg 768 Val Val Asn Pro Asp Asn Leu Thr Glu Trp Thr Tyr Ile Gly Pro Leu 245 250 255 ctt cat gtt ggc ttg aat tat cga ccc tct cga tgg tcg ggg gat ctc 816 Leu His Val Gly Leu Asn Tyr Arg Pro Ser Arg Trp Ser Gly Asp Leu 260 265 270 ggc gtc aac tgg gaa gtt gcc aac ttc ttt acg ttg aca gat ggc ggc 864 Gly Val Asn Trp Glu Val Ala Asn Phe Phe Thr Leu Thr Asp Gly Gly 275 280 285 gtc tcc cgg gat atc gtg atc ttc ggc gca gag gga tgc ttg tct tgc 912 Val Ser Arg Asp Ile Val Ile Phe Gly Ala Glu Gly Cys Leu Ser Cys 290 295 300 gag gtt gga tca aag aga gta ccg cgc tct ttg ctc tgg atg tgc att 960 Glu Val Gly Ser Lys Arg Val Pro Arg Ser Leu Leu Trp Met Cys Ile 305 310 315 320 aat gtc cga cct gga ctg cag gcg caa agc agt ggc gag cct ctc gca 1008 Asn Val Arg Pro Gly Leu Gln Ala Gln Ser Ser Gly Glu Pro Leu Ala 325 330 335 gat tat tca ttc tcg ggg atc ttc gat cac ggg tgc tgc tac gct gca 1056 Asp Tyr Ser Phe Ser Gly Ile Phe Asp His Gly Cys Cys Tyr Ala Ala 340 345 350 aac tct ttc tgg gac ccg gtc acg gag gag tat gtc gta tac tgc tgg 1104 Asn Ser Phe Trp Asp Pro Val Thr Glu Glu Tyr Val Val Tyr Cys Trp 355 360 365 att aca gag gag gat tta cca gat cgc ctg cgc cat cga caa ggc tgg 1152 Ile Thr Glu Glu Asp Leu Pro Asp Arg Leu Arg His Arg Gln Gly Trp 370 375 380 agt ggc atc atg tct cta ccg cga cta gta agg ctg gtg act ctt cac 1200 Ser Gly Ile Met Ser Leu Pro Arg Leu Val Arg Leu Val Thr Leu His 385 390 395 400 aat gtc aag cga gcc cac cag tca aag ctg gaa tcc att acg tct gtc 1248 Asn Val Lys Arg Ala His Gln Ser Lys Leu Glu Ser Ile Thr Ser Val 405 410 415 gaa ata gag cgc cat tcg caa ggt act cag gtc cga acc ttg agt gtc 1296 Glu Ile Glu Arg His Ser Gln Gly Thr Gln Val Arg Thr Leu Ser Val 420 425 430 cgg cct gac ccc agg ctc aac ata ctt cga aca tcg gct cga gag ctg 1344 Arg Pro Asp Pro Arg Leu Asn Ile Leu Arg Thr Ser Ala Arg Glu Leu 435 440 445 cat tta tcc aat gta caa ctg ggc tct gtg gcc cat cag ccc ccg gca 1392 His Leu Ser Asn Val Gln Leu Gly Ser Val Ala His Gln Pro Pro Ala 450 455 460 ttc ttg ccc ctg cgc act gct agg tgg gaa atg acc gcg act ttc gtg 1440 Phe Leu Pro Leu Arg Thr Ala Arg Trp Glu Met Thr Ala Thr Phe Val 465 470 475 480 att ggg acg cat tgc gcg gca gta gga ttg gaa atc ggc cat agc cct 1488 Ile Gly Thr His Cys Ala Ala Val Gly Leu Glu Ile Gly His Ser Pro 485 490 495 gaa gat ttc cac cag cgc acc acc cta tca tgg ata cca tac gac gag 1536 Glu Asp Phe His Gln Arg Thr Thr Leu Ser Trp Ile Pro Tyr Asp Glu 500 505 510 acg ttc aca atc gaa cgg cct ccg ctt cac gat gcc ggt atc aac cat 1584 Thr Phe Thr Ile Glu Arg Pro Pro Leu His Asp Ala Gly Ile Asn His 515 520 525 gtc ccc gag acc gct ccg cat act ctc ttc acc ttc tgc aac aat gaa 1632 Val Pro Glu Thr Ala Pro His Thr Leu Phe Thr Phe Cys Asn Asn Glu 530 535 540 ggc gag gag gtg acg gaa ccg ctt cag atc cac gcc tat ttc gat gca 1680 Gly Glu Glu Val Thr Glu Pro Leu Gln Ile His Ala Tyr Phe Asp Ala 545 550 555 560 agt gtg cta gaa gtg ttt gtg aat agc agg aca gtc atc tcc aca cgc 1728 Ser Val Leu Glu Val Phe Val Asn Ser Arg Thr Val Ile Ser Thr Arg 565 570 575 atc tat aca ccc cac gcg cag gtc tgc acg ggg ctg aaa ttc ttc gcc 1776 Ile Tyr Thr Pro His Ala Gln Val Cys Thr Gly Leu Lys Phe Phe Ala 580 585 590 tcg gca acc gaa agt cag ccg aaa cca tca aca tct gct cct gct gct 1824 Ser Ala Thr Glu Ser Gln Pro Lys Pro Ser Thr Ser Ala Pro Ala Ala 595 600 605 gtg ctg gtg aga gca gat att tgg gat gga ctg agt gtg att cgt gat 1872 Val Leu Val Arg Ala Asp Ile Trp Asp Gly Leu Ser Val Ile Arg Asp 610 615 620 gaa att aag cat tag 1887 Glu Ile Lys His * 625 36 628 PRT Aspergillus 36 Met His Ile Leu Pro Gly Ser Gln His Ala Ala Glu Leu Asp Asn Ser 1 5 10 15 Gly Thr Leu Ile His Ser Val His Cys Asp Pro Glu Gln Lys Ala Lys 20 25 30 Asn Ile Pro Gln Ser Thr Gly Ile Ala Gln Ala Ser Ser Glu Trp Arg 35 40 45 Pro Ser Tyr His Leu Ala Ala Pro Arg Gly Trp Met Asn Asp Pro Cys 50 55 60 Gly Leu Gly Tyr Asp Pro Thr Thr Gly Leu Tyr His Leu Ser Phe Gln 65 70 75 80 Trp Asn Pro His Gly Asn Asp Trp Gly Asn Ile Ser Trp Gly His Ala 85 90 95 Thr Ser Ser Asp Leu Val Ser Trp Gln Ile Ser Pro Glu Pro Cys Leu 100 105 110 Thr Pro Ser Ala Glu Tyr Asp Arg Cys Gly Val Phe Thr Gly Cys Phe 115 120 125 Arg Ser His Gly Pro Asp Gly Lys Pro Gly Val Leu Thr Tyr Val Tyr 130 135 140 Thr Ser Val Asn His Leu Pro Leu His Tyr Thr Leu Pro Tyr Val Lys 145 150 155 160 Gly Ser Glu Ser Leu Ser Ile Ala Val Ser Arg Asp His Gly Lys Thr 165 170 175 Trp Gln Arg Ile Asp Ser Asn Pro Ile His Pro Gly Ala Pro Ala Gly 180 185 190 Leu Glu Val Thr Gly Trp Arg Asp Pro Tyr Leu Asn Cys Trp Pro Ser 195 200 205 Leu Arg Ala Gln Arg Gln Gly Gly Val Ala Ser Pro Asp Leu Tyr Gly 210 215 220 Phe Ile Ser Gly Gly Ile Ala Lys Glu Ser Pro Thr Val Phe Val Tyr 225 230 235 240 Val Val Asn Pro Asp Asn Leu Thr Glu Trp Thr Tyr Ile Gly Pro Leu 245 250 255 Leu His Val Gly Leu Asn Tyr Arg Pro Ser Arg Trp Ser Gly Asp Leu 260 265 270 Gly Val Asn Trp Glu Val Ala Asn Phe Phe Thr Leu Thr Asp Gly Gly 275 280 285 Val Ser Arg Asp Ile Val Ile Phe Gly Ala Glu Gly Cys Leu Ser Cys 290 295 300 Glu Val Gly Ser Lys Arg Val Pro Arg Ser Leu Leu Trp Met Cys Ile 305 310 315 320 Asn Val Arg Pro Gly Leu Gln Ala Gln Ser Ser Gly Glu Pro Leu Ala 325 330 335 Asp Tyr Ser Phe Ser Gly Ile Phe Asp His Gly Cys Cys Tyr Ala Ala 340 345 350 Asn Ser Phe Trp Asp Pro Val Thr Glu Glu Tyr Val Val Tyr Cys Trp 355 360 365 Ile Thr Glu Glu Asp Leu Pro Asp Arg Leu Arg His Arg Gln Gly Trp 370 375 380 Ser Gly Ile Met Ser Leu Pro Arg Leu Val Arg Leu Val Thr Leu His 385 390 395 400 Asn Val Lys Arg Ala His Gln Ser Lys Leu Glu Ser Ile Thr Ser Val 405 410 415 Glu Ile Glu Arg His Ser Gln Gly Thr Gln Val Arg Thr Leu Ser Val 420 425 430 Arg Pro Asp Pro Arg Leu Asn Ile Leu Arg Thr Ser Ala Arg Glu Leu 435 440 445 His Leu Ser Asn Val Gln Leu Gly Ser Val Ala His Gln Pro Pro Ala 450 455 460 Phe Leu Pro Leu Arg Thr Ala Arg Trp Glu Met Thr Ala Thr Phe Val 465 470 475 480 Ile Gly Thr His Cys Ala Ala Val Gly Leu Glu Ile Gly His Ser Pro 485 490 495 Glu Asp Phe His Gln Arg Thr Thr Leu Ser Trp Ile Pro Tyr Asp Glu 500 505 510 Thr Phe Thr Ile Glu Arg Pro Pro Leu His Asp Ala Gly Ile Asn His 515 520 525 Val Pro Glu Thr Ala Pro His Thr Leu Phe Thr Phe Cys Asn Asn Glu 530 535 540 Gly Glu Glu Val Thr Glu Pro Leu Gln Ile His Ala Tyr Phe Asp Ala 545 550 555 560 Ser Val Leu Glu Val Phe Val Asn Ser Arg Thr Val Ile Ser Thr Arg 565 570 575 Ile Tyr Thr Pro His Ala Gln Val Cys Thr Gly Leu Lys Phe Phe Ala 580 585 590 Ser Ala Thr Glu Ser Gln Pro Lys Pro Ser Thr Ser Ala Pro Ala Ala 595 600 605 Val Leu Val Arg Ala Asp Ile Trp Asp Gly Leu Ser Val Ile Arg Asp 610 615 620 Glu Ile Lys His 625 37 1050 DNA Aspergillus 37 atggttcact ttaagtctgt ctgtacgctg gctgttacgg cgtttgctgc gctgggtgct 60 gcggcgccag caatgttggc aaagcgaggt atgtctgacg cttcctacga ttgggctatg 120 tgcgatgcta actattaagt agacgtgtcc tcgtcggtgc tgcaaaaact gtcactgttt 180 gcgcaatact ctgctgcctc ctattgtacc aacaacatca attccacggg caacaagctg 240 acatgctcct ctggagagtg cccgctggtc gaggcagcca acaccaagac cctttcggaa 300 ttctacgagt aggtcgatcc catgcatgag tagctcgtat ctctaacaga gttggtagtg 360 attccgcgta tggagacgtc gcaggcttct tggttgcaga caccacgaac aagctacttg 420 tggtctcttt cagaggaagc cgcacgatag acacatggtt ggcgaacctg gactttggcc 480 tggacagtat cagtgatgtt tgcagcggat gtgcggtaca taagggattc tggaagtcct 540 gggaagtcgt tgccaatgca ctaacgaccg agctaaactc tgcccttgca acttacagtg 600 gctataccgt tgtctttact ggccatagct tcggcgctgc tcttgcaacg ctgggggctg 660 ctacgttgcg gaaagcaggg attcccgtag agctggtaag tcatcccttg tcaaatcagg 720 taagggcgta atgggactaa ttgattgaag tatggttacg gatccccgcg tgttggaaat 780 aaggccttgg caacattcat caccggacag ggttccaatt accgtgtcac acacacaaac 840 gacattgtcc ccagactccc gccccgagtc tttggcttca gccacattag cccagagtac 900 tggatcacga gcggtgacaa cgctcctgtc acgacgtctg atgtcacggt tgtccaggga 960 atcgactcaa gcggtggaaa tgcgggcgag gattctacca gcattgaggc ccataattgg 1020 tatattggcc atattgatgg ttgtcaataa 1050 38 900 DNA Aspergillus CDS (1)...(900) 38 atg gtt cac ttt aag tct gtc tgt acg ctg gct gtt acg gcg ttt gct 48 Met Val His Phe Lys Ser Val Cys Thr Leu Ala Val Thr Ala Phe Ala 1 5 10 15 gcg ctg ggt gct gcg gcg cca gca atg ttg gca aag cga gac gtg tcc 96 Ala Leu Gly Ala Ala Ala Pro Ala Met Leu Ala Lys Arg Asp Val Ser 20 25 30 tcg tcg gtg ctg caa aaa ctg tca ctg ttt gcg caa tac tct gct gcc 144 Ser Ser Val Leu Gln Lys Leu Ser Leu Phe Ala Gln Tyr Ser Ala Ala 35 40 45 tcc tat tgt acc aac aac atc aat tcc acg ggc aac aag ctg aca tgc 192 Ser Tyr Cys Thr Asn Asn Ile Asn Ser Thr Gly Asn Lys Leu Thr Cys 50 55 60 tcc tct gga gag tgc ccg ctg gtc gag gca gcc aac acc aag acc ctt 240 Ser Ser Gly Glu Cys Pro Leu Val Glu Ala Ala Asn Thr Lys Thr Leu 65 70 75 80 tcg gaa ttc tac gaa gtt ggt agt gat tcc gcg tat gga gac gtc gca 288 Ser Glu Phe Tyr Glu Val Gly Ser Asp Ser Ala Tyr Gly Asp Val Ala 85 90 95 ggc ttc ttg gtt gca gac acc acg aac aag cta ctt gtg gtc tct ttc 336 Gly Phe Leu Val Ala Asp Thr Thr Asn Lys Leu Leu Val Val Ser Phe 100 105 110 aga gga agc cgc acg ata gac aca tgg ttg gcg aac ctg gac ttt ggc 384 Arg Gly Ser Arg Thr Ile Asp Thr Trp Leu Ala Asn Leu Asp Phe Gly 115 120 125 ctg gac agt atc agt gat gtt tgc agc gga tgt gcg gta cat aag gga 432 Leu Asp Ser Ile Ser Asp Val Cys Ser Gly Cys Ala Val His Lys Gly 130 135 140 ttc tgg aag tcc tgg gaa gtc gtt gcc aat gca cta acg acc gag cta 480 Phe Trp Lys Ser Trp Glu Val Val Ala Asn Ala Leu Thr Thr Glu Leu 145 150 155 160 aac tct gcc ctt gca act tac agt ggc tat acc gtt gtc ttt act ggc 528 Asn Ser Ala Leu Ala Thr Tyr Ser Gly Tyr Thr Val Val Phe Thr Gly 165 170 175 cat agc ttc ggc gct gct ctt gca acg ctg ggg gct gct acg ttg cgg 576 His Ser Phe Gly Ala Ala Leu Ala Thr Leu Gly Ala Ala Thr Leu Arg 180 185 190 aaa gca ggg att ccc gta gag ctg tat ggt tac gga tcc ccg cgt gtt 624 Lys Ala Gly Ile Pro Val Glu Leu Tyr Gly Tyr Gly Ser Pro Arg Val 195 200 205 gga aat aag gcc ttg gca aca ttc atc acc gga cag ggt tcc aat tac 672 Gly Asn Lys Ala Leu Ala Thr Phe Ile Thr Gly Gln Gly Ser Asn Tyr 210 215 220 cgt gtc aca cac aca aac gac att gtc ccc aga ctc ccg ccc cga gtc 720 Arg Val Thr His Thr Asn Asp Ile Val Pro Arg Leu Pro Pro Arg Val 225 230 235 240 ttt ggc ttc agc cac att agc cca gag tac tgg atc acg agc ggt gac 768 Phe Gly Phe Ser His Ile Ser Pro Glu Tyr Trp Ile Thr Ser Gly Asp 245 250 255 aac gct cct gtc acg acg tct gat gtc acg gtt gtc cag gga atc gac 816 Asn Ala Pro Val Thr Thr Ser Asp Val Thr Val Val Gln Gly Ile Asp 260 265 270 tca agc ggt gga aat gcg ggc gag gat tct acc agc att gag gcc cat 864 Ser Ser Gly Gly Asn Ala Gly Glu Asp Ser Thr Ser Ile Glu Ala His 275 280 285 aat tgg tat att ggc cat att gat ggt tgt caa taa 900 Asn Trp Tyr Ile Gly His Ile Asp Gly Cys Gln * 290 295 39 299 PRT Aspergillus 39 Met Val His Phe Lys Ser Val Cys Thr Leu Ala Val Thr Ala Phe Ala 1 5 10 15 Ala Leu Gly Ala Ala Ala Pro Ala Met Leu Ala Lys Arg Asp Val Ser 20 25 30 Ser Ser Val Leu Gln Lys Leu Ser Leu Phe Ala Gln Tyr Ser Ala Ala 35 40 45 Ser Tyr Cys Thr Asn Asn Ile Asn Ser Thr Gly Asn Lys Leu Thr Cys 50 55 60 Ser Ser Gly Glu Cys Pro Leu Val Glu Ala Ala Asn Thr Lys Thr Leu 65 70 75 80 Ser Glu Phe Tyr Glu Val Gly Ser Asp Ser Ala Tyr Gly Asp Val Ala 85 90 95 Gly Phe Leu Val Ala Asp Thr Thr Asn Lys Leu Leu Val Val Ser Phe 100 105 110 Arg Gly Ser Arg Thr Ile Asp Thr Trp Leu Ala Asn Leu Asp Phe Gly 115 120 125 Leu Asp Ser Ile Ser Asp Val Cys Ser Gly Cys Ala Val His Lys Gly 130 135 140 Phe Trp Lys Ser Trp Glu Val Val Ala Asn Ala Leu Thr Thr Glu Leu 145 150 155 160 Asn Ser Ala Leu Ala Thr Tyr Ser Gly Tyr Thr Val Val Phe Thr Gly 165 170 175 His Ser Phe Gly Ala Ala Leu Ala Thr Leu Gly Ala Ala Thr Leu Arg 180 185 190 Lys Ala Gly Ile Pro Val Glu Leu Tyr Gly Tyr Gly Ser Pro Arg Val 195 200 205 Gly Asn Lys Ala Leu Ala Thr Phe Ile Thr Gly Gln Gly Ser Asn Tyr 210 215 220 Arg Val Thr His Thr Asn Asp Ile Val Pro Arg Leu Pro Pro Arg Val 225 230 235 240 Phe Gly Phe Ser His Ile Ser Pro Glu Tyr Trp Ile Thr Ser Gly Asp 245 250 255 Asn Ala Pro Val Thr Thr Ser Asp Val Thr Val Val Gln Gly Ile Asp 260 265 270 Ser Ser Gly Gly Asn Ala Gly Glu Asp Ser Thr Ser Ile Glu Ala His 275 280 285 Asn Trp Tyr Ile Gly His Ile Asp Gly Cys Gln 290 295 40 1926 DNA Aspergillus 40 atgcatatac gctggtcatc cttttttctt tcttgccttg ctggaacagc tttggcggcc 60 actccagcgc aatggcgatc ccagtccatc tatttcttac tcacggatcg attcgcaagg 120 actgacggtt ccacaacggc ctcgtgtgat actagtgctc gagtcagcta cacgagcctc 180 ccttcacaag ccacagtgta ctgacacgtg aaataggagt attgtggtgg tacatggcaa 240 ggcattattg aacaagtcag aactagtgtg gagagtaaga gtgtaacaat ggctgattgg 300 gtcaatatag ctcgattaca tacaaggcat gggctttaca gcaatttgga taaccccagt 360 caccaagcaa cttccccagg atacgtcgga aggcactgca taccacgggt actggcagca 420 agacatgtga gcatcaagtc atccccacag tctcgtatta gctttttgct gactcggtaa 480 gttattcggt caattccaac tatgggaccg ctgacgacct gaaagccctg gcgtcagctc 540 ttcatgacag gggcatgtat ctcatggtcg atgttgttgc caatcacatg gttcgctgga 600 tcagcccatt gatgtgctgc ttgctgattg aaccagggat atgccggtgc aggcgattcg 660 gtcgactata gtgtcttcaa ccccttcaac tcccagacct ccttccaccc attgtgcttc 720 atcagcaatt acgataatca gacagacgtg gaaaattgct ggttggggga caattcggtt 780 cctttacccg atcttgatac tacaaatccg gatgttcaaa agatttggta caattgggtg 840 aactctttag tgtctaatta ttccagtaag gacggactct tggtatctgc acaaaaacaa 900 gaattgactg atatgctaca gtcgacggcc tacgaattga cactgtgaag cacgtccaga 960 gcgatttctg gccgggattc aatgacgccg caggcgtcta ctgtatcggg gaggtatttg 1020 atggagatcc agcgtacact tgtccctacc aagaggtcct ggacggggtg ctgaattacc 1080 ctatgtaagt cgcataagca tatgaacctg tccatggctg cggatctaat tagagcagat 1140 attatccgct tctgaaagcc ttccaatcca caagtggcag tatgagcagc ctctacgata 1200 tgatcaacac ggtcaagtcg cagtgcgccg attcgacgct gttgggcacc tttgtcgaaa 1260 atcacgatac tccccggttc gcatcgtaag tttcttccta gactcattgt cattccagcg 1320 tcctgatgaa tccccgctcg caggtatacc aaggacatgg ccctcgctaa aaacgccgca 1380 gcattcatca tcttctccga tggaatccca atcatctacg ccggccagga gcaacattac 1440 agcggcggcg cggatcccgc aaaccgtgag gcagtctggc tatccggcta ctcgacaacg 1500 agtgacctat acaagctcat cgcgacagca aacgccatcc ggagtcacgc cattagcaag 1560 gacccgggat acgtgactta taaggtacga ggctctcact cacggaagga ccatacgatc 1620 aagcagggct tactcaaccc acagaataac cccatctaca aagatacctc caccatcgcc 1680 atgcgaaaag gctccgacgg agcgcagatc atcaccgtcc tctcgaacct cggtgcttct 1740 ggaagctctt acacgctctc attgggtgga acaggctatg aggccggaca acaactgact 1800 gagatgttct cctgcaccac ggtgaccgtg ggctcagaca aaaaggtccc cgtttccatg 1860 gctagtggct tgccccgggt gttttaccca acggctgggc tgaacggaag tactgtttgt 1920 acttga 1926 41 1488 DNA Aspergillus CDS (1)...(1488) 41 atg cat ata cgc tgg tca tcc ttt ttt ctt tct tgc ctt gct gga aca 48 Met His Ile Arg Trp Ser Ser Phe Phe Leu Ser Cys Leu Ala Gly Thr 1 5 10 15 gct ttg gcg gcc act cca gcg caa tgg cga tcc cag tcc atc tat ttc 96 Ala Leu Ala Ala Thr Pro Ala Gln Trp Arg Ser Gln Ser Ile Tyr Phe 20 25 30 tta ctc acg gat cga ttc gca agg act gac ggt tcc aca acg gcc tcg 144 Leu Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser 35 40 45 tgt gat act agt gct cga gag tat tgt ggt ggt aca tgg caa ggc att 192 Cys Asp Thr Ser Ala Arg Glu Tyr Cys Gly Gly Thr Trp Gln Gly Ile 50 55 60 att gaa caa ctc gat tac ata caa ggc atg ggc ttt aca gca att tgg 240 Ile Glu Gln Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp 65 70 75 80 ata acc cca gtc acc aag caa ctt ccc cag gat acg tcg gaa ggc act 288 Ile Thr Pro Val Thr Lys Gln Leu Pro Gln Asp Thr Ser Glu Gly Thr 85 90 95 gca tac cac ggg tac tgg cag caa gac att tat tcg gtc aat tcc aac 336 Ala Tyr His Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Val Asn Ser Asn 100 105 110 tat ggg acc gct gac gac ctg aaa gcc ctg gcg tca gct ctt cat gac 384 Tyr Gly Thr Ala Asp Asp Leu Lys Ala Leu Ala Ser Ala Leu His Asp 115 120 125 agg ggc atg tat ctc atg gtc gat gtt gtt gcc aat cac atg gga tat 432 Arg Gly Met Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr 130 135 140 gcc ggt gca ggc gat tcg gtc gac tat agt gtc ttc aac ccc ttc aac 480 Ala Gly Ala Gly Asp Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn 145 150 155 160 tcc cag acc tcc ttc cac cca ttg tgc ttc atc agc aat tac gat aat 528 Ser Gln Thr Ser Phe His Pro Leu Cys Phe Ile Ser Asn Tyr Asp Asn 165 170 175 cag aca gac gtg gaa aat tgc tgg ttg ggg gac aat tcg gtt cct tta 576 Gln Thr Asp Val Glu Asn Cys Trp Leu Gly Asp Asn Ser Val Pro Leu 180 185 190 ccc gat ctt gat act aca aat ccg gat gtt caa aag att tgg tac aat 624 Pro Asp Leu Asp Thr Thr Asn Pro Asp Val Gln Lys Ile Trp Tyr Asn 195 200 205 tgg gtg aac tct tta gtg tct aat tat tcc atc gac ggc cta cga att 672 Trp Val Asn Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile 210 215 220 gac act gtg aag cac gtc cag agc gat ttc tgg ccg gga ttc aat gac 720 Asp Thr Val Lys His Val Gln Ser Asp Phe Trp Pro Gly Phe Asn Asp 225 230 235 240 gcc gca ggc gtc tac tgt atc ggg gag gta ttt gat gga gat cca gcg 768 Ala Ala Gly Val Tyr Cys Ile Gly Glu Val Phe Asp Gly Asp Pro Ala 245 250 255 tac act tgt ccc tac caa gag gtc ctg gac ggg gtg ctg aat tac cct 816 Tyr Thr Cys Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro 260 265 270 ata tat tat ccg ctt ctg aaa gcc ttc caa tcc aca agt ggc agt atg 864 Ile Tyr Tyr Pro Leu Leu Lys Ala Phe Gln Ser Thr Ser Gly Ser Met 275 280 285 agc agc ctc tac gat atg atc aac acg gtc aag tcg cag tgc gcc gat 912 Ser Ser Leu Tyr Asp Met Ile Asn Thr Val Lys Ser Gln Cys Ala Asp 290 295 300 tcg acg ctg ttg ggc acc ttt gtc gaa aat cac gat act ccc cgg ttc 960 Ser Thr Leu Leu Gly Thr Phe Val Glu Asn His Asp Thr Pro Arg Phe 305 310 315 320 gca tcg tat acc aag gac atg gcc ctc gct aaa aac gcc gca gca ttc 1008 Ala Ser Tyr Thr Lys Asp Met Ala Leu Ala Lys Asn Ala Ala Ala Phe 325 330 335 atc atc ttc tcc gat gga atc cca atc atc tac gcc ggc cag gag caa 1056 Ile Ile Phe Ser Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln 340 345 350 cat tac agc ggc ggc gcg gat ccc gca aac cgt gag gca gtc tgg cta 1104 His Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Ala Val Trp Leu 355 360 365 tcc ggc tac tcg aca acg agt gac cta tac aag ctc atc gcg aca gca 1152 Ser Gly Tyr Ser Thr Thr Ser Asp Leu Tyr Lys Leu Ile Ala Thr Ala 370 375 380 aac gcc atc cgg agt cac gcc att agc aag gac ccg gga tac gtg act 1200 Asn Ala Ile Arg Ser His Ala Ile Ser Lys Asp Pro Gly Tyr Val Thr 385 390 395 400 tat aag aat aac ccc atc tac aaa gat acc tcc acc atc gcc atg cga 1248 Tyr Lys Asn Asn Pro Ile Tyr Lys Asp Thr Ser Thr Ile Ala Met Arg 405 410 415 aaa ggc tcc gac gga gcg cag atc atc acc gtc ctc tcg aac ctc ggt 1296 Lys Gly Ser Asp Gly Ala Gln Ile Ile Thr Val Leu Ser Asn Leu Gly 420 425 430 gct tct gga agc tct tac acg ctc tca ttg ggt gga aca ggc tat gag 1344 Ala Ser Gly Ser Ser Tyr Thr Leu Ser Leu Gly Gly Thr Gly Tyr Glu 435 440 445 gcc gga caa caa ctg act gag atg ttc tcc tgc acc acg gtg acc gtg 1392 Ala Gly Gln Gln Leu Thr Glu Met Phe Ser Cys Thr Thr Val Thr Val 450 455 460 ggc tca gac aaa aag gtc ccc gtt tcc atg gct agt ggc ttg ccc cgg 1440 Gly Ser Asp Lys Lys Val Pro Val Ser Met Ala Ser Gly Leu Pro Arg 465 470 475 480 gtg ttt tac cca acg gct ggg ctg aac gga agt act gtt tgt act tga 1488 Val Phe Tyr Pro Thr Ala Gly Leu Asn Gly Ser Thr Val Cys Thr * 485 490 495 42 495 PRT Aspergillus 42 Met His Ile Arg Trp Ser Ser Phe Phe Leu Ser Cys Leu Ala Gly Thr 1 5 10 15 Ala Leu Ala Ala Thr Pro Ala Gln Trp Arg Ser Gln Ser Ile Tyr Phe 20 25 30 Leu Leu Thr Asp Arg Phe Ala Arg Thr Asp Gly Ser Thr Thr Ala Ser 35 40 45 Cys Asp Thr Ser Ala Arg Glu Tyr Cys Gly Gly Thr Trp Gln Gly Ile 50 55 60 Ile Glu Gln Leu Asp Tyr Ile Gln Gly Met Gly Phe Thr Ala Ile Trp 65 70 75 80 Ile Thr Pro Val Thr Lys Gln Leu Pro Gln Asp Thr Ser Glu Gly Thr 85 90 95 Ala Tyr His Gly Tyr Trp Gln Gln Asp Ile Tyr Ser Val Asn Ser Asn 100 105 110 Tyr Gly Thr Ala Asp Asp Leu Lys Ala Leu Ala Ser Ala Leu His Asp 115 120 125 Arg Gly Met Tyr Leu Met Val Asp Val Val Ala Asn His Met Gly Tyr 130 135 140 Ala Gly Ala Gly Asp Ser Val Asp Tyr Ser Val Phe Asn Pro Phe Asn 145 150 155 160 Ser Gln Thr Ser Phe His Pro Leu Cys Phe Ile Ser Asn Tyr Asp Asn 165 170 175 Gln Thr Asp Val Glu Asn Cys Trp Leu Gly Asp Asn Ser Val Pro Leu 180 185 190 Pro Asp Leu Asp Thr Thr Asn Pro Asp Val Gln Lys Ile Trp Tyr Asn 195 200 205 Trp Val Asn Ser Leu Val Ser Asn Tyr Ser Ile Asp Gly Leu Arg Ile 210 215 220 Asp Thr Val Lys His Val Gln Ser Asp Phe Trp Pro Gly Phe Asn Asp 225 230 235 240 Ala Ala Gly Val Tyr Cys Ile Gly Glu Val Phe Asp Gly Asp Pro Ala 245 250 255 Tyr Thr Cys Pro Tyr Gln Glu Val Leu Asp Gly Val Leu Asn Tyr Pro 260 265 270 Ile Tyr Tyr Pro Leu Leu Lys Ala Phe Gln Ser Thr Ser Gly Ser Met 275 280 285 Ser Ser Leu Tyr Asp Met Ile Asn Thr Val Lys Ser Gln Cys Ala Asp 290 295 300 Ser Thr Leu Leu Gly Thr Phe Val Glu Asn His Asp Thr Pro Arg Phe 305 310 315 320 Ala Ser Tyr Thr Lys Asp Met Ala Leu Ala Lys Asn Ala Ala Ala Phe 325 330 335 Ile Ile Phe Ser Asp Gly Ile Pro Ile Ile Tyr Ala Gly Gln Glu Gln 340 345 350 His Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu Ala Val Trp Leu 355 360 365 Ser Gly Tyr Ser Thr Thr Ser Asp Leu Tyr Lys Leu Ile Ala Thr Ala 370 375 380 Asn Ala Ile Arg Ser His Ala Ile Ser Lys Asp Pro Gly Tyr Val Thr 385 390 395 400 Tyr Lys Asn Asn Pro Ile Tyr Lys Asp Thr Ser Thr Ile Ala Met Arg 405 410 415 Lys Gly Ser Asp Gly Ala Gln Ile Ile Thr Val Leu Ser Asn Leu Gly 420 425 430 Ala Ser Gly Ser Ser Tyr Thr Leu Ser Leu Gly Gly Thr Gly Tyr Glu 435 440 445 Ala Gly Gln Gln Leu Thr Glu Met Phe Ser Cys Thr Thr Val Thr Val 450 455 460 Gly Ser Asp Lys Lys Val Pro Val Ser Met Ala Ser Gly Leu Pro Arg 465 470 475 480 Val Phe Tyr Pro Thr Ala Gly Leu Asn Gly Ser Thr Val Cys Thr 485 490 495 43 2250 DNA Aspergillus 43 atgaagtgga tctcgcagct cttcccgttg tccctgtgct cgtccctgct cggacaggct 60 gcccatgctc tgaccccagc cgaatggcgc agtcaatcga tctatttcct cctgaccgat 120 cggttcggcc gagaagacaa ttccacgact gctgcctgcg atgtcacgca acgagtgtgt 180 ccccctatcg ttcttgatcg agctcatgct aacatttgca gctgtattgc ggcgggagct 240 ggcaggggat catcaatcat gtacgactgt cccatatcgc gcggtcgaaa ctaacaatgt 300 cagctcgact acattcaagg catgggattt actgccatat ggatcacccc cgtaactgag 360 cagttctatg agaacaccgg cgatggtact tcgtaccatg gatactggca gcagaatatg 420 tgagttctct ttggccgcgg tgattcatac taatcgacga agccacgagg tcaatgccaa 480 ttatggaacg gcacaagatc ttagagatct ggccaacgct ctgcacgcgc gtggcatgta 540 cttgatggtc gatgtggtcg ccaaccatat ggtacgccgt cttctcgagt tgtacattat 600 aatctgactg gttaagggct acaacggagc gggaaactcg gtcaactacg gtgtcttcac 660 tccgtttgat tccgctacct atttccaccc atactgtctc atcaccgact acaacaacca 720 aacagctgtg gaggactgct ggctgggaga tactactgtc tcgctacccg atctcgacac 780 gaccagcacg gcagtgcgaa gcatctggta tgattgggtg aagggattgg ttgccaacta 840 ctccagtcag tgagagccgc atccgagcgt gaatgatact gaccgagata gtcgacggcc 900 tgcgcatcga cacggtgaag catgtcgaga aagacttctg gcccggctac aatgacgctg 960 ctggcgtcta ctgtgtcggt gaagtctttt cgggtgatcc acaatatacc tgtccatacc 1020 agaattacct ggatggtgta ctcaactacc ccatgtacgc attatgattt ccgtacggat 1080 ttgatcctga cgagagcaga tactatcaac ttctctacgc gttccaatcg accagcggca 1140 gcatcagcaa tctgtacaac atgatcagct ccgttgcgtc tgactgtgcg gatcccactt 1200 tgctcggcaa ctttatcgag aaccatgata acccccgatt tgcctcgtaa gaccgtgcct 1260 ccgttccctg aatgcaacta acctccccag ctatacgagc gactattcgc aagccaagaa 1320 cgtcatctcc ttcatgttct tctccgacgg catccccatt gtctacgccg gacaggagca 1380 gcactacagc ggcggtgctg accctgccaa ccgcgaggct gtctggctgt ctggatactc 1440 gaccagcgct acgctgtaca gctggattgc ctctaccaac aagattcgca agctagcgat 1500 ttccaaagac tcagcctaca taacatccaa ggtatttccg gtcacgtctt cgcattccac 1560 cgctaacatc gatagaacaa cccgttctac tatgattcca atactctcgc tatgcgcaag 1620 ggctcagtcg ctggctctca agtcattacc gtcctcagta acaagggatc ctcgggcagt 1680 tcctacaccc tctctctcag cggcacgggc tactccgccg gcgccaccct tgtcgagatg 1740 tatacatgca ctactctcac cgtggactcg agcggaaatc tcgccgtgcc aatggtatcc 1800 ggcttgccca gagttttcgt gccctcgtca tgggtcagtg ggagtggcct ctgcggcgac 1860 tctatctcca ccacggcgac cgcccccagt gccaccacga gcgcaacagc gacaagaaca 1920 gcatgcgcag ctgccacagc cattccgatt ctcttcgagg agctcgtgac aactacctac 1980 ggcgagtcca tctacctgac cggctcgatc agccaactcg ggaactggga cacgagttct 2040 gcgattgctc tgtcggcgag taaatacacc tcgtcgaacc ctgagtggta tgtcaccgtg 2100 accctgcctg ttggcacctc atttgagtac aaattcgtca agaaggggtc ggatgggagc 2160 atcgcgtggg aaagtgatcc gaaccggtcg tatacggtgc cgactgggtg tgcgggaacg 2220 accgtgacgg tgtctgatac gtggagatga 2250 44 1893 DNA Aspergillus CDS (1)...(1893) 44 atg aag tgg atc tcg cag ctc ttc ccg ttg tcc ctg tgc tcg tcc ctg 48 Met Lys Trp Ile Ser Gln Leu Phe Pro Leu Ser Leu Cys Ser Ser Leu 1 5 10 15 ctc gga cag gct gcc cat gct ctg acc cca gcc gaa tgg cgc agt caa 96 Leu Gly Gln Ala Ala His Ala Leu Thr Pro Ala Glu Trp Arg Ser Gln 20 25 30 tcg atc tat ttc ctc ctg acc gat cgg ttc ggc cga gaa gac aat tcc 144 Ser Ile Tyr Phe Leu Leu Thr Asp Arg Phe Gly Arg Glu Asp Asn Ser 35 40 45 acg act gct gcc tgc gat gtc acg caa cga ctg tat tgc ggc ggg agc 192 Thr Thr Ala Ala Cys Asp Val Thr Gln Arg Leu Tyr Cys Gly Gly Ser 50 55 60 tgg cag ggg atc atc aat cat ctc gac tac att caa ggc atg gga ttt 240 Trp Gln Gly Ile Ile Asn His Leu Asp Tyr Ile Gln Gly Met Gly Phe 65 70 75 80 act gcc ata tgg atc acc ccc gta act gag cag ttc tat gag aac acc 288 Thr Ala Ile Trp Ile Thr Pro Val Thr Glu Gln Phe Tyr Glu Asn Thr 85 90 95 ggc gat ggt act tcg tac cat gga tac tgg cag cag aat atc cac gag 336 Gly Asp Gly Thr Ser Tyr His Gly Tyr Trp Gln Gln Asn Ile His Glu 100 105 110 gtc aat gcc aat tat gga acg gca caa gat ctt aga gat ctg gcc aac 384 Val Asn Ala Asn Tyr Gly Thr Ala Gln Asp Leu Arg Asp Leu Ala Asn 115 120 125 gct ctg cac gcg cgt ggc atg tac ttg atg gtc gat gtg gtc gcc aac 432 Ala Leu His Ala Arg Gly Met Tyr Leu Met Val Asp Val Val Ala Asn 130 135 140 cat atg ggc tac aac gga gcg gga aac tcg gtc aac tac ggt gtc ttc 480 His Met Gly Tyr Asn Gly Ala Gly Asn Ser Val Asn Tyr Gly Val Phe 145 150 155 160 act ccg ttt gat tcc gct acc tat ttc cac cca tac tgt ctc atc acc 528 Thr Pro Phe Asp Ser Ala Thr Tyr Phe His Pro Tyr Cys Leu Ile Thr 165 170 175 gac tac aac aac caa aca gct gtg gag gac tgc tgg ctg gga gat act 576 Asp Tyr Asn Asn Gln Thr Ala Val Glu Asp Cys Trp Leu Gly Asp Thr 180 185 190 act gtc tcg cta ccc gat ctc gac acg acc agc acg gca gtg cga agc 624 Thr Val Ser Leu Pro Asp Leu Asp Thr Thr Ser Thr Ala Val Arg Ser 195 200 205 atc tgg tat gat tgg gtg aag gga ttg gtt gcc aac tac tcc atc gac 672 Ile Trp Tyr Asp Trp Val Lys Gly Leu Val Ala Asn Tyr Ser Ile Asp 210 215 220 ggc ctg cgc atc gac acg gtg aag cat gtc gag aaa gac ttc tgg ccc 720 Gly Leu Arg Ile Asp Thr Val Lys His Val Glu Lys Asp Phe Trp Pro 225 230 235 240 ggc tac aat gac gct gct ggc gtc tac tgt gtc ggt gaa gtc ttt tcg 768 Gly Tyr Asn Asp Ala Ala Gly Val Tyr Cys Val Gly Glu Val Phe Ser 245 250 255 ggt gat cca caa tat acc tgt cca tac cag aat tac ctg gat ggt gta 816 Gly Asp Pro Gln Tyr Thr Cys Pro Tyr Gln Asn Tyr Leu Asp Gly Val 260 265 270 ctc aac tac ccc ata tac tat caa ctt ctc tac gcg ttc caa tcg acc 864 Leu Asn Tyr Pro Ile Tyr Tyr Gln Leu Leu Tyr Ala Phe Gln Ser Thr 275 280 285 agc ggc agc atc agc aat ctg tac aac atg atc agc tcc gtt gcg tct 912 Ser Gly Ser Ile Ser Asn Leu Tyr Asn Met Ile Ser Ser Val Ala Ser 290 295 300 gac tgt gcg gat ccc act ttg ctc ggc aac ttt atc gag aac cat gat 960 Asp Cys Ala Asp Pro Thr Leu Leu Gly Asn Phe Ile Glu Asn His Asp 305 310 315 320 aac ccc cga ttt gcc tcc tat acg agc gac tat tcg caa gcc aag aac 1008 Asn Pro Arg Phe Ala Ser Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn 325 330 335 gtc atc tcc ttc atg ttc ttc tcc gac ggc atc ccc att gtc tac gcc 1056 Val Ile Ser Phe Met Phe Phe Ser Asp Gly Ile Pro Ile Val Tyr Ala 340 345 350 gga cag gag cag cac tac agc ggc ggt gct gac cct gcc aac cgc gag 1104 Gly Gln Glu Gln His Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu 355 360 365 gct gtc tgg ctg tct gga tac tcg acc agc gct acg ctg tac agc tgg 1152 Ala Val Trp Leu Ser Gly Tyr Ser Thr Ser Ala Thr Leu Tyr Ser Trp 370 375 380 att gcc tct acc aac aag att cgc aag cta gcg att tcc aaa gac tca 1200 Ile Ala Ser Thr Asn Lys Ile Arg Lys Leu Ala Ile Ser Lys Asp Ser 385 390 395 400 gcc tac ata aca tcc aag aac aac ccg ttc tac tat gat tcc aat act 1248 Ala Tyr Ile Thr Ser Lys Asn Asn Pro Phe Tyr Tyr Asp Ser Asn Thr 405 410 415 ctc gct atg cgc aag ggc tca gtc gct ggc tct caa gtc att acc gtc 1296 Leu Ala Met Arg Lys Gly Ser Val Ala Gly Ser Gln Val Ile Thr Val 420 425 430 ctc agt aac aag gga tcc tcg ggc agt tcc tac acc ctc tct ctc agc 1344 Leu Ser Asn Lys Gly Ser Ser Gly Ser Ser Tyr Thr Leu Ser Leu Ser 435 440 445 ggc acg ggc tac tcc gcc ggc gcc acc ctt gtc gag atg tat aca tgc 1392 Gly Thr Gly Tyr Ser Ala Gly Ala Thr Leu Val Glu Met Tyr Thr Cys 450 455 460 act act ctc acc gtg gac tcg agc gga aat ctc gcc gtg cca atg gta 1440 Thr Thr Leu Thr Val Asp Ser Ser Gly Asn Leu Ala Val Pro Met Val 465 470 475 480 tcc ggc ttg ccc aga gtt ttc gtg ccc tcg tca tgg gtc agt ggg agt 1488 Ser Gly Leu Pro Arg Val Phe Val Pro Ser Ser Trp Val Ser Gly Ser 485 490 495 ggc ctc tgc ggc gac tct atc tcc acc acg gcg acc gcc ccc agt gcc 1536 Gly Leu Cys Gly Asp Ser Ile Ser Thr Thr Ala Thr Ala Pro Ser Ala 500 505 510 acc acg agc gca aca gcg aca aga aca gca tgc gca gct gcc aca gcc 1584 Thr Thr Ser Ala Thr Ala Thr Arg Thr Ala Cys Ala Ala Ala Thr Ala 515 520 525 att ccg att ctc ttc gag gag ctc gtg aca act acc tac ggc gag tcc 1632 Ile Pro Ile Leu Phe Glu Glu Leu Val Thr Thr Thr Tyr Gly Glu Ser 530 535 540 atc tac ctg acc ggc tcg atc agc caa ctc ggg aac tgg gac acg agt 1680 Ile Tyr Leu Thr Gly Ser Ile Ser Gln Leu Gly Asn Trp Asp Thr Ser 545 550 555 560 tct gcg att gct ctg tcg gcg agt aaa tac acc tcg tcg aac cct gag 1728 Ser Ala Ile Ala Leu Ser Ala Ser Lys Tyr Thr Ser Ser Asn Pro Glu 565 570 575 tgg tat gtc acc gtg acc ctg cct gtt ggc acc tca ttt gag tac aaa 1776 Trp Tyr Val Thr Val Thr Leu Pro Val Gly Thr Ser Phe Glu Tyr Lys 580 585 590 ttc gtc aag aag ggg tcg gat ggg agc atc gcg tgg gaa agt gat ccg 1824 Phe Val Lys Lys Gly Ser Asp Gly Ser Ile Ala Trp Glu Ser Asp Pro 595 600 605 aac cgg tcg tat acg gtg ccg act ggg tgt gcg gga acg acc gtg acg 1872 Asn Arg Ser Tyr Thr Val Pro Thr Gly Cys Ala Gly Thr Thr Val Thr 610 615 620 gtg tct gat acg tgg aga tga 1893 Val Ser Asp Thr Trp Arg * 625 630 45 630 PRT Aspergillus 45 Met Lys Trp Ile Ser Gln Leu Phe Pro Leu Ser Leu Cys Ser Ser Leu 1 5 10 15 Leu Gly Gln Ala Ala His Ala Leu Thr Pro Ala Glu Trp Arg Ser Gln 20 25 30 Ser Ile Tyr Phe Leu Leu Thr Asp Arg Phe Gly Arg Glu Asp Asn Ser 35 40 45 Thr Thr Ala Ala Cys Asp Val Thr Gln Arg Leu Tyr Cys Gly Gly Ser 50 55 60 Trp Gln Gly Ile Ile Asn His Leu Asp Tyr Ile Gln Gly Met Gly Phe 65 70 75 80 Thr Ala Ile Trp Ile Thr Pro Val Thr Glu Gln Phe Tyr Glu Asn Thr 85 90 95 Gly Asp Gly Thr Ser Tyr His Gly Tyr Trp Gln Gln Asn Ile His Glu 100 105 110 Val Asn Ala Asn Tyr Gly Thr Ala Gln Asp Leu Arg Asp Leu Ala Asn 115 120 125 Ala Leu His Ala Arg Gly Met Tyr Leu Met Val Asp Val Val Ala Asn 130 135 140 His Met Gly Tyr Asn Gly Ala Gly Asn Ser Val Asn Tyr Gly Val Phe 145 150 155 160 Thr Pro Phe Asp Ser Ala Thr Tyr Phe His Pro Tyr Cys Leu Ile Thr 165 170 175 Asp Tyr Asn Asn Gln Thr Ala Val Glu Asp Cys Trp Leu Gly Asp Thr 180 185 190 Thr Val Ser Leu Pro Asp Leu Asp Thr Thr Ser Thr Ala Val Arg Ser 195 200 205 Ile Trp Tyr Asp Trp Val Lys Gly Leu Val Ala Asn Tyr Ser Ile Asp 210 215 220 Gly Leu Arg Ile Asp Thr Val Lys His Val Glu Lys Asp Phe Trp Pro 225 230 235 240 Gly Tyr Asn Asp Ala Ala Gly Val Tyr Cys Val Gly Glu Val Phe Ser 245 250 255 Gly Asp Pro Gln Tyr Thr Cys Pro Tyr Gln Asn Tyr Leu Asp Gly Val 260 265 270 Leu Asn Tyr Pro Ile Tyr Tyr Gln Leu Leu Tyr Ala Phe Gln Ser Thr 275 280 285 Ser Gly Ser Ile Ser Asn Leu Tyr Asn Met Ile Ser Ser Val Ala Ser 290 295 300 Asp Cys Ala Asp Pro Thr Leu Leu Gly Asn Phe Ile Glu Asn His Asp 305 310 315 320 Asn Pro Arg Phe Ala Ser Tyr Thr Ser Asp Tyr Ser Gln Ala Lys Asn 325 330 335 Val Ile Ser Phe Met Phe Phe Ser Asp Gly Ile Pro Ile Val Tyr Ala 340 345 350 Gly Gln Glu Gln His Tyr Ser Gly Gly Ala Asp Pro Ala Asn Arg Glu 355 360 365 Ala Val Trp Leu Ser Gly Tyr Ser Thr Ser Ala Thr Leu Tyr Ser Trp 370 375 380 Ile Ala Ser Thr Asn Lys Ile Arg Lys Leu Ala Ile Ser Lys Asp Ser 385 390 395 400 Ala Tyr Ile Thr Ser Lys Asn Asn Pro Phe Tyr Tyr Asp Ser Asn Thr 405 410 415 Leu Ala Met Arg Lys Gly Ser Val Ala Gly Ser Gln Val Ile Thr Val 420 425 430 Leu Ser Asn Lys Gly Ser Ser Gly Ser Ser Tyr Thr Leu Ser Leu Ser 435 440 445 Gly Thr Gly Tyr Ser Ala Gly Ala Thr Leu Val Glu Met Tyr Thr Cys 450 455 460 Thr Thr Leu Thr Val Asp Ser Ser Gly Asn Leu Ala Val Pro Met Val 465 470 475 480 Ser Gly Leu Pro Arg Val Phe Val Pro Ser Ser Trp Val Ser Gly Ser 485 490 495 Gly Leu Cys Gly Asp Ser Ile Ser Thr Thr Ala Thr Ala Pro Ser Ala 500 505 510 Thr Thr Ser Ala Thr Ala Thr Arg Thr Ala Cys Ala Ala Ala Thr Ala 515 520 525 Ile Pro Ile Leu Phe Glu Glu Leu Val Thr Thr Thr Tyr Gly Glu Ser 530 535 540 Ile Tyr Leu Thr Gly Ser Ile Ser Gln Leu Gly Asn Trp Asp Thr Ser 545 550 555 560 Ser Ala Ile Ala Leu Ser Ala Ser Lys Tyr Thr Ser Ser Asn Pro Glu 565 570 575 Trp Tyr Val Thr Val Thr Leu Pro Val Gly Thr Ser Phe Glu Tyr Lys 580 585 590 Phe Val Lys Lys Gly Ser Asp Gly Ser Ile Ala Trp Glu Ser Asp Pro 595 600 605 Asn Arg Ser Tyr Thr Val Pro Thr Gly Cys Ala Gly Thr Thr Val Thr 610 615 620 Val Ser Asp Thr Trp Arg 625 630 46 1707 DNA Aspergillus 46 atgatatact cgctgcgaat cctgcagtgg ctttgcatca ctgcagggct tgacctgctc 60 gtgccatcct tggctgcaga tacaagtgca tggaagtcca ggtctatcta tcagacgatg 120 acagacagat ttgcacgtac ggatgggtcc accactcatc catgcaacac cacagaaggg 180 ctacgctgtg gtggctcatg gagaggtaca atccaacacc tcgattacat tcaaggaatg 240 ggattcgacg ctatcatgat ctccccaatc gtccagaatg tcgaggggcg cgtgcagtac 300 ggagaggcct atcatggcta ctgggtccag gacatgtatg cgctaaaccc acactttggc 360 actcaccagg acctgttaga cttgagtaag gctgttcatg atcggggcat gtatctgatg 420 gtagatactg tcatcaacaa cttggcgtac atcaccgacg gacgaaaccc ggccacgagc 480 attgactatt cagcgctcag accattcaat gactcaatgt tctttcatcc atattgcaag 540 atcaccgact atgacaacta tccattggcg caaacatgct ggacaggtga tgatgttgtt 600 ccccttccag atctaaagac agaagatagc caagttcaga gcatgctcat ggactggatt 660 agaaaaatga tggctacgta ttcaatcgat ggcctacgtc tggatgctgc gaagcatatt 720 acaccaagtt tcttgccttt gttccaaaac gcttctggcg cttttattac tggagaagtt 780 ttcgagccgt ccgtgaagac gatctgcgga tatcaaaagg acctccccag cgtccccaat 840 tatcccatct attattccat cttggaggca tttacgaaag gcaacacaag ctctctgacg 900 aatcaggtag aggtcatgaa acagacatgt tctgatgtta ctgcccttac ttcgttctcg 960 gagaatcatg acgtcgctcg atttgcaagc ttcaaggatg acatcgcggt aaggcagcga 1020 actccagtta ccctgaaagt atcaaccgat gataggctaa caccggcgca gctcgctaag 1080 aacgttttaa catttacgat gctgttcgac ggcataccga tgatatacca agggcaagaa 1140 caacatttct caggcgccag tgacccggag aaccgcgaag ccttatggct atcaggctac 1200 aacaccaacg ctccgcttta ccaactagcc acgagactga acaggatccg caagcatgca 1260 gcccagatcg acccagcatt tgtagactca cagaccttcc ccatctacac agggtctagc 1320 gagatgggtt tccgcaaagg cgtcgagggc cggcaactcg taatggtctt gtcaactcaa 1380 ggtatggaca gcggcaaata tgagctggac atgccaatag gctaccaacc tggatttgtg 1440 gtcacagatg tgcttaattg cgccaactat tcggttaacg acatgggtct tctcaaggtc 1500 agcatggata agggcgagcc tcgggtcctt tttcccgctg acatgatgga aggaagtggt 1560 ctatgcggat atggaaggtc gaatggaacg acgtatctta atctgaaaaa gaattcaacg 1620 cagttctcgg gtggcgggct ctcaaatcgg cctaccgtgc ccctactgtt gatctgttgt 1680 ttgacttgct tgatactatg gtgttga 1707 47 1644 DNA Aspergillus CDS (1)...(1644) 47 atg ata tac tcg ctg cga atc ctg cag tgg ctt tgc atc act gca ggg 48 Met Ile Tyr Ser Leu Arg Ile Leu Gln Trp Leu Cys Ile Thr Ala Gly 1 5 10 15 ctt gac ctg ctc gtg cca tcc ttg gct gca gat aca agt gca tgg aag 96 Leu Asp Leu Leu Val Pro Ser Leu Ala Ala Asp Thr Ser Ala Trp Lys 20 25 30 tcc agg tct atc tat cag acg atg aca gac aga ttt gca cgt acg gat 144 Ser Arg Ser Ile Tyr Gln Thr Met Thr Asp Arg Phe Ala Arg Thr Asp 35 40 45 ggg tcc acc act cat cca tgc aac acc aca gaa ggg cta cgc tgt ggt 192 Gly Ser Thr Thr His Pro Cys Asn Thr Thr Glu Gly Leu Arg Cys Gly 50 55 60 ggc tca tgg aga ggt aca atc caa cac ctc gat tac att caa gga atg 240 Gly Ser Trp Arg Gly Thr Ile Gln His Leu Asp Tyr Ile Gln Gly Met 65 70 75 80 gga ttc gac gct atc atg atc tcc cca atc gtc cag aat gtc gag ggg 288 Gly Phe Asp Ala Ile Met Ile Ser Pro Ile Val Gln Asn Val Glu Gly 85 90 95 cgc gtg cag tac gga gag gcc tat cat ggc tac tgg gtc cag gac atg 336 Arg Val Gln Tyr Gly Glu Ala Tyr His Gly Tyr Trp Val Gln Asp Met 100 105 110 tat gcg cta aac cca cac ttt ggc act cac cag gac ctg tta gac ttg 384 Tyr Ala Leu Asn Pro His Phe Gly Thr His Gln Asp Leu Leu Asp Leu 115 120 125 agt aag gct gtt cat gat cgg ggc atg tat ctg atg gta gat act gtc 432 Ser Lys Ala Val His Asp Arg Gly Met Tyr Leu Met Val Asp Thr Val 130 135 140 atc aac aac ttg gcg tac atc acc gac gga cga aac ccg gcc acg agc 480 Ile Asn Asn Leu Ala Tyr Ile Thr Asp Gly Arg Asn Pro Ala Thr Ser 145 150 155 160 att gac tat tca gcg ctc aga cca ttc aat gac tca atg ttc ttt cat 528 Ile Asp Tyr Ser Ala Leu Arg Pro Phe Asn Asp Ser Met Phe Phe His 165 170 175 cca tat tgc aag atc acc gac tat gac aac tat cca ttg gcg caa aca 576 Pro Tyr Cys Lys Ile Thr Asp Tyr Asp Asn Tyr Pro Leu Ala Gln Thr 180 185 190 tgc tgg aca ggt gat gat gtt gtt ccc ctt cca gat cta aag aca gaa 624 Cys Trp Thr Gly Asp Asp Val Val Pro Leu Pro Asp Leu Lys Thr Glu 195 200 205 gat agc caa gtt cag agc atg ctc atg gac tgg att aga aaa atg atg 672 Asp Ser Gln Val Gln Ser Met Leu Met Asp Trp Ile Arg Lys Met Met 210 215 220 gct acg tat tca atc gat ggc cta cgt ctg gat gct gcg aag cat att 720 Ala Thr Tyr Ser Ile Asp Gly Leu Arg Leu Asp Ala Ala Lys His Ile 225 230 235 240 aca cca agt ttc ttg cct ttg ttc caa aac gct tct ggc gct ttt att 768 Thr Pro Ser Phe Leu Pro Leu Phe Gln Asn Ala Ser Gly Ala Phe Ile 245 250 255 act gga gaa gtt ttc gag ccg tcc gtg aag acg atc tgc gga tat caa 816 Thr Gly Glu Val Phe Glu Pro Ser Val Lys Thr Ile Cys Gly Tyr Gln 260 265 270 aag gac ctc ccc agc gtc ccc aat tat ccc atc tat tat tcc atc ttg 864 Lys Asp Leu Pro Ser Val Pro Asn Tyr Pro Ile Tyr Tyr Ser Ile Leu 275 280 285 gag gca ttt acg aaa ggc aac aca agc tct ctg acg aat cag gta gag 912 Glu Ala Phe Thr Lys Gly Asn Thr Ser Ser Leu Thr Asn Gln Val Glu 290 295 300 gtc atg aaa cag aca tgt tct gat gtt act gcc ctt act tcg ttc tcg 960 Val Met Lys Gln Thr Cys Ser Asp Val Thr Ala Leu Thr Ser Phe Ser 305 310 315 320 gag aat cat gac gtc gct cga ttt gca agc ttc aag gat gac atc gcg 1008 Glu Asn His Asp Val Ala Arg Phe Ala Ser Phe Lys Asp Asp Ile Ala 325 330 335 ctc gct aag aac gtt tta aca ttt acg atg ctg ttc gac ggc ata ccg 1056 Leu Ala Lys Asn Val Leu Thr Phe Thr Met Leu Phe Asp Gly Ile Pro 340 345 350 atg ata tac caa ggg caa gaa caa cat ttc tca ggc gcc agt gac ccg 1104 Met Ile Tyr Gln Gly Gln Glu Gln His Phe Ser Gly Ala Ser Asp Pro 355 360 365 gag aac cgc gaa gcc tta tgg cta tca ggc tac aac acc aac gct ccg 1152 Glu Asn Arg Glu Ala Leu Trp Leu Ser Gly Tyr Asn Thr Asn Ala Pro 370 375 380 ctt tac caa cta gcc acg aga ctg aac agg atc cgc aag cat gca gcc 1200 Leu Tyr Gln Leu Ala Thr Arg Leu Asn Arg Ile Arg Lys His Ala Ala 385 390 395 400 cag atc gac cca gca ttt gta gac tca cag acc ttc ccc atc tac aca 1248 Gln Ile Asp Pro Ala Phe Val Asp Ser Gln Thr Phe Pro Ile Tyr Thr 405 410 415 ggg tct agc gag atg ggt ttc cgc aaa ggc gtc gag ggc cgg caa ctc 1296 Gly Ser Ser Glu Met Gly Phe Arg Lys Gly Val Glu Gly Arg Gln Leu 420 425 430 gta atg gtc ttg tca act caa ggt atg gac agc ggc aaa tat gag ctg 1344 Val Met Val Leu Ser Thr Gln Gly Met Asp Ser Gly Lys Tyr Glu Leu 435 440 445 gac atg cca ata ggc tac caa cct gga ttt gtg gtc aca gat gtg ctt 1392 Asp Met Pro Ile Gly Tyr Gln Pro Gly Phe Val Val Thr Asp Val Leu 450 455 460 aat tgc gcc aac tat tcg gtt aac gac atg ggt ctt ctc aag gtc agc 1440 Asn Cys Ala Asn Tyr Ser Val Asn Asp Met Gly Leu Leu Lys Val Ser 465 470 475 480 atg gat aag ggc gag cct cgg gtc ctt ttt ccc gct gac atg atg gaa 1488 Met Asp Lys Gly Glu Pro Arg Val Leu Phe Pro Ala Asp Met Met Glu 485 490 495 gga agt ggt cta tgc gga tat gga agg tcg aat gga acg acg tat ctt 1536 Gly Ser Gly Leu Cys Gly Tyr Gly Arg Ser Asn Gly Thr Thr Tyr Leu 500 505 510 aat ctg aaa aag aat tca acg cag ttc tcg ggt ggc ggg ctc tca aat 1584 Asn Leu Lys Lys Asn Ser Thr Gln Phe Ser Gly Gly Gly Leu Ser Asn 515 520 525 cgg cct acc gtg ccc cta ctg ttg atc tgt tgt ttg act tgc ttg ata 1632 Arg Pro Thr Val Pro Leu Leu Leu Ile Cys Cys Leu Thr Cys Leu Ile 530 535 540 cta tgg tgt tga 1644 Leu Trp Cys * 545 48 547 PRT Aspergillus 48 Met Ile Tyr Ser Leu Arg Ile Leu Gln Trp Leu Cys Ile Thr Ala Gly 1 5 10 15 Leu Asp Leu Leu Val Pro Ser Leu Ala Ala Asp Thr Ser Ala Trp Lys 20 25 30 Ser Arg Ser Ile Tyr Gln Thr Met Thr Asp Arg Phe Ala Arg Thr Asp 35 40 45 Gly Ser Thr Thr His Pro Cys Asn Thr Thr Glu Gly Leu Arg Cys Gly 50 55 60 Gly Ser Trp Arg Gly Thr Ile Gln His Leu Asp Tyr Ile Gln Gly Met 65 70 75 80 Gly Phe Asp Ala Ile Met Ile Ser Pro Ile Val Gln Asn Val Glu Gly 85 90 95 Arg Val Gln Tyr Gly Glu Ala Tyr His Gly Tyr Trp Val Gln Asp Met 100 105 110 Tyr Ala Leu Asn Pro His Phe Gly Thr His Gln Asp Leu Leu Asp Leu 115 120 125 Ser Lys Ala Val His Asp Arg Gly Met Tyr Leu Met Val Asp Thr Val 130 135 140 Ile Asn Asn Leu Ala Tyr Ile Thr Asp Gly Arg Asn Pro Ala Thr Ser 145 150 155 160 Ile Asp Tyr Ser Ala Leu Arg Pro Phe Asn Asp Ser Met Phe Phe His 165 170 175 Pro Tyr Cys Lys Ile Thr Asp Tyr Asp Asn Tyr Pro Leu Ala Gln Thr 180 185 190 Cys Trp Thr Gly Asp Asp Val Val Pro Leu Pro Asp Leu Lys Thr Glu 195 200 205 Asp Ser Gln Val Gln Ser Met Leu Met Asp Trp Ile Arg Lys Met Met 210 215 220 Ala Thr Tyr Ser Ile Asp Gly Leu Arg Leu Asp Ala Ala Lys His Ile 225 230 235 240 Thr Pro Ser Phe Leu Pro Leu Phe Gln Asn Ala Ser Gly Ala Phe Ile 245 250 255 Thr Gly Glu Val Phe Glu Pro Ser Val Lys Thr Ile Cys Gly Tyr Gln 260 265 270 Lys Asp Leu Pro Ser Val Pro Asn Tyr Pro Ile Tyr Tyr Ser Ile Leu 275 280 285 Glu Ala Phe Thr Lys Gly Asn Thr Ser Ser Leu Thr Asn Gln Val Glu 290 295 300 Val Met Lys Gln Thr Cys Ser Asp Val Thr Ala Leu Thr Ser Phe Ser 305 310 315 320 Glu Asn His Asp Val Ala Arg Phe Ala Ser Phe Lys Asp Asp Ile Ala 325 330 335 Leu Ala Lys Asn Val Leu Thr Phe Thr Met Leu Phe Asp Gly Ile Pro 340 345 350 Met Ile Tyr Gln Gly Gln Glu Gln His Phe Ser Gly Ala Ser Asp Pro 355 360 365 Glu Asn Arg Glu Ala Leu Trp Leu Ser Gly Tyr Asn Thr Asn Ala Pro 370 375 380 Leu Tyr Gln Leu Ala Thr Arg Leu Asn Arg Ile Arg Lys His Ala Ala 385 390 395 400 Gln Ile Asp Pro Ala Phe Val Asp Ser Gln Thr Phe Pro Ile Tyr Thr 405 410 415 Gly Ser Ser Glu Met Gly Phe Arg Lys Gly Val Glu Gly Arg Gln Leu 420 425 430 Val Met Val Leu Ser Thr Gln Gly Met Asp Ser Gly Lys Tyr Glu Leu 435 440 445 Asp Met Pro Ile Gly Tyr Gln Pro Gly Phe Val Val Thr Asp Val Leu 450 455 460 Asn Cys Ala Asn Tyr Ser Val Asn Asp Met Gly Leu Leu Lys Val Ser 465 470 475 480 Met Asp Lys Gly Glu Pro Arg Val Leu Phe Pro Ala Asp Met Met Glu 485 490 495 Gly Ser Gly Leu Cys Gly Tyr Gly Arg Ser Asn Gly Thr Thr Tyr Leu 500 505 510 Asn Leu Lys Lys Asn Ser Thr Gln Phe Ser Gly Gly Gly Leu Ser Asn 515 520 525 Arg Pro Thr Val Pro Leu Leu Leu Ile Cys Cys Leu Thr Cys Leu Ile 530 535 540 Leu Trp Cys 545 49 1906 DNA Aspergillus 49 atgggcttct ttcgcgatgg actgacttcc ttaggcctgc ttctgttatg ctttgtttca 60 tggggatcag ctggtgtggt gcgcttcaaa atcacactga catgggagga ctggactccg 120 actggtattg cgcggaaaat gattctcacc aatggccaat ttccagctcc gccattgtac 180 gtgcgacagg gcgatgatgt cgagtttttg gtagataatc aacttccctt tgctaccgca 240 gtccatttcc acggtaaagc ttgttcactg acagcaattg ctagccaagg ctgacacctc 300 acctcaatca ggtattgacc aaatggggac gccatggtcc gatggagttc ctggtctttc 360 gcaaagaccc attccgtccg gcagcagttt tctttacaaa tggaatgcgg gacagtatgg 420 cagctatatg tatcacgctc acagcagagg gcagattgat gatggcttat acggagcgat 480 ttatatccgt cctggtgacg aagtggagaa acccttttgg ttgataagta atcgtacacg 540 tgaagtcaag gccatgcgac gagccgaaga aaggacaacc cccatagtgc tgagtgactg 600 gcgccagttg acgtccgagg agctgtggca tgcggaagag gcaactggac tagacgcata 660 ctgtgtgaat gcgctattag tcaatggaag gggctccgta cagtgtctag accgcagtac 720 gttggatcgg tatagcgcgg caaagtgggc atttttggga aactcttcgc tgactgatat 780 tgggtaagag tgaaaaaaat acggcgattc gacatattga tctgaagctg actctcccag 840 ctgcgcgccc ccgacgattc ctctgctcca aggggacttt ccacacaact ttagtgccac 900 gccaccgaca ctgttttctg gctgtactcc gtctcaggga tcgacggagc tactcctcgt 960 tgatccacaa gcttcgtacg ccagctttga cctgattagt gctgctggtg tgtcgatgcc 1020 tactttctca atcgacgaac atcccatgta tatatacgcc atcgatggaa gatatatcgt 1080 cccggttcga gtggatgcca tcaccatcgg caatggaaac cgttattcgg tcatggtgaa 1140 actggataaa ccggctggtg attacaccgt gcgtgtagcg aacgccggaa tcaaccaact 1200 tattactgct aatgcgagca tgtcttacaa cacgcttttc agggctcaat cacgtccttc 1260 gcagccatca atcgacatca ccggcgcaaa cacaacagcg gacgtcgtga tcctcgacga 1320 gagcagggtg atccctttcc ctgtggaggt accggcgcaa gacgttgccc agaccttctt 1380 cctagatgtc gcccggttca acgcgtccta ccggtggatt cttggaagct cggacttccc 1440 gctctccgtg gaggaatcgc ccccacttct gttcaatcgc tccgccgcca agcccgatct 1500 ttcgatttca acgcgtaacg gaacttgggt cgatctcatc ttcagagtca ccggcccttt 1560 acagccacca caccctattc acaagcactc gaacaagttc ttcgtcattg gtcaagggaa 1620 cggtgtcttc aattatacct cagtgactga ggcgcggaaa cacattccgg aaagcttcaa 1680 tcttaatgcc ccgcagatac gggacacgtt cgcgacgcct cccagtgtat ccggccccac 1740 ttggttggca ataagatatc atgtcgtgaa tcctggcgca ttcttgatcc attgtcacat 1800 ccaaatccat ctgagcggtg gtatggcgct ggcaatattg gacggcgtag ataagtggcc 1860 tgtggacatt ccccaggagt accagcttgc ggcctcagga tcatag 1906 50 1791 DNA aspergillus CDS (1)...(1791) 50 atg ggc ttc ttt cgc gat gga ctg act tcc tta ggc ctg ctt ctg tta 48 Met Gly Phe Phe Arg Asp Gly Leu Thr Ser Leu Gly Leu Leu Leu Leu 1 5 10 15 tgc ttt gtt tca tgg gga tca gct ggt gtg gtg cgc ttc aaa atc aca 96 Cys Phe Val Ser Trp Gly Ser Ala Gly Val Val Arg Phe Lys Ile Thr 20 25 30 ctg aca tgg gag gac tgg act ccg act ggt att gcg cgg aaa atg att 144 Leu Thr Trp Glu Asp Trp Thr Pro Thr Gly Ile Ala Arg Lys Met Ile 35 40 45 ctc acc aat ggc caa ttt cca gct ccg cca ttg tac gtg cga cag ggc 192 Leu Thr Asn Gly Gln Phe Pro Ala Pro Pro Leu Tyr Val Arg Gln Gly 50 55 60 gat gat gtc gag ttt ttg gta gat aat caa ctt ccc ttt gct acc gca 240 Asp Asp Val Glu Phe Leu Val Asp Asn Gln Leu Pro Phe Ala Thr Ala 65 70 75 80 gtc cat ttc cac ggt att gac caa atg ggg acg cca tgg tcc gat gga 288 Val His Phe His Gly Ile Asp Gln Met Gly Thr Pro Trp Ser Asp Gly 85 90 95 gtt cct ggt ctt tcg caa aga ccc att ccg tcc ggc agc agt ttt ctt 336 Val Pro Gly Leu Ser Gln Arg Pro Ile Pro Ser Gly Ser Ser Phe Leu 100 105 110 tac aaa tgg aat gcg gga cag tat ggc agc tat atg tat cac gct cac 384 Tyr Lys Trp Asn Ala Gly Gln Tyr Gly Ser Tyr Met Tyr His Ala His 115 120 125 agc aga ggg cag att gat gat ggc tta tac gga gcg att tat atc cgt 432 Ser Arg Gly Gln Ile Asp Asp Gly Leu Tyr Gly Ala Ile Tyr Ile Arg 130 135 140 cct ggt gac gaa gtg gag aaa ccc ttt tgg ttg ata agt aat cgt aca 480 Pro Gly Asp Glu Val Glu Lys Pro Phe Trp Leu Ile Ser Asn Arg Thr 145 150 155 160 cgt gaa gtc aag gcc atg cga cga gcc gaa gaa agg aca acc ccc ata 528 Arg Glu Val Lys Ala Met Arg Arg Ala Glu Glu Arg Thr Thr Pro Ile 165 170 175 gtg ctg agt gac tgg cgc cag ttg acg tcc gag gag ctg tgg cat gcg 576 Val Leu Ser Asp Trp Arg Gln Leu Thr Ser Glu Glu Leu Trp His Ala 180 185 190 gaa gag gca act gga cta gac gca tac tgt gtg aat gcg cta tta gtc 624 Glu Glu Ala Thr Gly Leu Asp Ala Tyr Cys Val Asn Ala Leu Leu Val 195 200 205 aat gga agg ggc tcc gta cag tgt cta gac cgc agt acg ttg gat cgg 672 Asn Gly Arg Gly Ser Val Gln Cys Leu Asp Arg Ser Thr Leu Asp Arg 210 215 220 tat agc gcg gca aag tgg gca ttt ttg gga aac tct tcg ctg act gat 720 Tyr Ser Ala Ala Lys Trp Ala Phe Leu Gly Asn Ser Ser Leu Thr Asp 225 230 235 240 att ggc tgc gcg ccc ccg acg att cct ctg ctc caa ggg gac ttt cca 768 Ile Gly Cys Ala Pro Pro Thr Ile Pro Leu Leu Gln Gly Asp Phe Pro 245 250 255 cac aac ttt agt gcc acg cca ccg aca ctg ttt tct ggc tgt act ccg 816 His Asn Phe Ser Ala Thr Pro Pro Thr Leu Phe Ser Gly Cys Thr Pro 260 265 270 tct cag gga tcg acg gag cta ctc ctc gtt gat cca caa gct tcg tac 864 Ser Gln Gly Ser Thr Glu Leu Leu Leu Val Asp Pro Gln Ala Ser Tyr 275 280 285 gcc agc ttt gac ctg att agt gct gct ggt gtg tcg atg cct act ttc 912 Ala Ser Phe Asp Leu Ile Ser Ala Ala Gly Val Ser Met Pro Thr Phe 290 295 300 tca atc gac gaa cat ccc atg tat ata tac gcc atc gat gga aga tat 960 Ser Ile Asp Glu His Pro Met Tyr Ile Tyr Ala Ile Asp Gly Arg Tyr 305 310 315 320 atc gtc ccg gtt cga gtg gat gcc atc acc atc ggc aat gga aac cgt 1008 Ile Val Pro Val Arg Val Asp Ala Ile Thr Ile Gly Asn Gly Asn Arg 325 330 335 tat tcg gtc atg gtg aaa ctg gat aaa ccg gct ggt gat tac acc gtg 1056 Tyr Ser Val Met Val Lys Leu Asp Lys Pro Ala Gly Asp Tyr Thr Val 340 345 350 cgt gta gcg aac gcc gga atc aac caa ctt att act gct aat gcg agc 1104 Arg Val Ala Asn Ala Gly Ile Asn Gln Leu Ile Thr Ala Asn Ala Ser 355 360 365 atg tct tac aac acg ctt ttc agg gct caa tca cgt cct tcg cag cca 1152 Met Ser Tyr Asn Thr Leu Phe Arg Ala Gln Ser Arg Pro Ser Gln Pro 370 375 380 tca atc gac atc acc ggc gca aac aca aca gcg gac gtc gtg atc ctc 1200 Ser Ile Asp Ile Thr Gly Ala Asn Thr Thr Ala Asp Val Val Ile Leu 385 390 395 400 gac gag agc agg gtg atc cct ttc cct gtg gag gta ccg gcg caa gac 1248 Asp Glu Ser Arg Val Ile Pro Phe Pro Val Glu Val Pro Ala Gln Asp 405 410 415 gtt gcc cag acc ttc ttc cta gat gtc gcc cgg ttc aac gcg tcc tac 1296 Val Ala Gln Thr Phe Phe Leu Asp Val Ala Arg Phe Asn Ala Ser Tyr 420 425 430 cgg tgg att ctt gga agc tcg gac ttc ccg ctc tcc gtg gag gaa tcg 1344 Arg Trp Ile Leu Gly Ser Ser Asp Phe Pro Leu Ser Val Glu Glu Ser 435 440 445 ccc cca ctt ctg ttc aat cgc tcc gcc gcc aag ccc gat ctt tcg att 1392 Pro Pro Leu Leu Phe Asn Arg Ser Ala Ala Lys Pro Asp Leu Ser Ile 450 455 460 tca acg cgt aac gga act tgg gtc gat ctc atc ttc aga gtc acc ggc 1440 Ser Thr Arg Asn Gly Thr Trp Val Asp Leu Ile Phe Arg Val Thr Gly 465 470 475 480 cct tta cag cca cca cac cct att cac aag cac tcg aac aag ttc ttc 1488 Pro Leu Gln Pro Pro His Pro Ile His Lys His Ser Asn Lys Phe Phe 485 490 495 gtc att ggt caa ggg aac ggt gtc ttc aat tat acc tca gtg act gag 1536 Val Ile Gly Gln Gly Asn Gly Val Phe Asn Tyr Thr Ser Val Thr Glu 500 505 510 gcg cgg aaa cac att ccg gaa agc ttc aat ctt aat gcc ccg cag ata 1584 Ala Arg Lys His Ile Pro Glu Ser Phe Asn Leu Asn Ala Pro Gln Ile 515 520 525 cgg gac acg ttc gcg acg cct ccc agt gta tcc ggc ccc act tgg ttg 1632 Arg Asp Thr Phe Ala Thr Pro Pro Ser Val Ser Gly Pro Thr Trp Leu 530 535 540 gca ata aga tat cat gtc gtg aat cct ggc gca ttc ttg atc cat tgt 1680 Ala Ile Arg Tyr His Val Val Asn Pro Gly Ala Phe Leu Ile His Cys 545 550 555 560 cac atc caa atc cat ctg agc ggt ggt atg gcg ctg gca ata ttg gac 1728 His Ile Gln Ile His Leu Ser Gly Gly Met Ala Leu Ala Ile Leu Asp 565 570 575 ggc gta gat aag tgg cct gtg gac att ccc cag gag tac cag ctt gcg 1776 Gly Val Asp Lys Trp Pro Val Asp Ile Pro Gln Glu Tyr Gln Leu Ala 580 585 590 gcc tca gga tca tag 1791 Ala Ser Gly Ser * 595 51 596 PRT aspergillus 51 Met Gly Phe Phe Arg Asp Gly Leu Thr Ser Leu Gly Leu Leu Leu Leu 1 5 10 15 Cys Phe Val Ser Trp Gly Ser Ala Gly Val Val Arg Phe Lys Ile Thr 20 25 30 Leu Thr Trp Glu Asp Trp Thr Pro Thr Gly Ile Ala Arg Lys Met Ile 35 40 45 Leu Thr Asn Gly Gln Phe Pro Ala Pro Pro Leu Tyr Val Arg Gln Gly 50 55 60 Asp Asp Val Glu Phe Leu Val Asp Asn Gln Leu Pro Phe Ala Thr Ala 65 70 75 80 Val His Phe His Gly Ile Asp Gln Met Gly Thr Pro Trp Ser Asp Gly 85 90 95 Val Pro Gly Leu Ser Gln Arg Pro Ile Pro Ser Gly Ser Ser Phe Leu 100 105 110 Tyr Lys Trp Asn Ala Gly Gln Tyr Gly Ser Tyr Met Tyr His Ala His 115 120 125 Ser Arg Gly Gln Ile Asp Asp Gly Leu Tyr Gly Ala Ile Tyr Ile Arg 130 135 140 Pro Gly Asp Glu Val Glu Lys Pro Phe Trp Leu Ile Ser Asn Arg Thr 145 150 155 160 Arg Glu Val Lys Ala Met Arg Arg Ala Glu Glu Arg Thr Thr Pro Ile 165 170 175 Val Leu Ser Asp Trp Arg Gln Leu Thr Ser Glu Glu Leu Trp His Ala 180 185 190 Glu Glu Ala Thr Gly Leu Asp Ala Tyr Cys Val Asn Ala Leu Leu Val 195 200 205 Asn Gly Arg Gly Ser Val Gln Cys Leu Asp Arg Ser Thr Leu Asp Arg 210 215 220 Tyr Ser Ala Ala Lys Trp Ala Phe Leu Gly Asn Ser Ser Leu Thr Asp 225 230 235 240 Ile Gly Cys Ala Pro Pro Thr Ile Pro Leu Leu Gln Gly Asp Phe Pro 245 250 255 His Asn Phe Ser Ala Thr Pro Pro Thr Leu Phe Ser Gly Cys Thr Pro 260 265 270 Ser Gln Gly Ser Thr Glu Leu Leu Leu Val Asp Pro Gln Ala Ser Tyr 275 280 285 Ala Ser Phe Asp Leu Ile Ser Ala Ala Gly Val Ser Met Pro Thr Phe 290 295 300 Ser Ile Asp Glu His Pro Met Tyr Ile Tyr Ala Ile Asp Gly Arg Tyr 305 310 315 320 Ile Val Pro Val Arg Val Asp Ala Ile Thr Ile Gly Asn Gly Asn Arg 325 330 335 Tyr Ser Val Met Val Lys Leu Asp Lys Pro Ala Gly Asp Tyr Thr Val 340 345 350 Arg Val Ala Asn Ala Gly Ile Asn Gln Leu Ile Thr Ala Asn Ala Ser 355 360 365 Met Ser Tyr Asn Thr Leu Phe Arg Ala Gln Ser Arg Pro Ser Gln Pro 370 375 380 Ser Ile Asp Ile Thr Gly Ala Asn Thr Thr Ala Asp Val Val Ile Leu 385 390 395 400 Asp Glu Ser Arg Val Ile Pro Phe Pro Val Glu Val Pro Ala Gln Asp 405 410 415 Val Ala Gln Thr Phe Phe Leu Asp Val Ala Arg Phe Asn Ala Ser Tyr 420 425 430 Arg Trp Ile Leu Gly Ser Ser Asp Phe Pro Leu Ser Val Glu Glu Ser 435 440 445 Pro Pro Leu Leu Phe Asn Arg Ser Ala Ala Lys Pro Asp Leu Ser Ile 450 455 460 Ser Thr Arg Asn Gly Thr Trp Val Asp Leu Ile Phe Arg Val Thr Gly 465 470 475 480 Pro Leu Gln Pro Pro His Pro Ile His Lys His Ser Asn Lys Phe Phe 485 490 495 Val Ile Gly Gln Gly Asn Gly Val Phe Asn Tyr Thr Ser Val Thr Glu 500 505 510 Ala Arg Lys His Ile Pro Glu Ser Phe Asn Leu Asn Ala Pro Gln Ile 515 520 525 Arg Asp Thr Phe Ala Thr Pro Pro Ser Val Ser Gly Pro Thr Trp Leu 530 535 540 Ala Ile Arg Tyr His Val Val Asn Pro Gly Ala Phe Leu Ile His Cys 545 550 555 560 His Ile Gln Ile His Leu Ser Gly Gly Met Ala Leu Ala Ile Leu Asp 565 570 575 Gly Val Asp Lys Trp Pro Val Asp Ile Pro Gln Glu Tyr Gln Leu Ala 580 585 590 Ala Ser Gly Ser 595 52 2060 DNA Aspergillus 52 atgcctcgcc tttcctacgc gctctgtgcg ctgtctctcg ggcatgctgc tattgcagct 60 cctcagttat ccgctcgtgc taccggcagc ttggactcct ggttgggtac tgagaccacc 120 gttgcgctca atggtattct ggccaacatc ggtgccgacg gtgcttatgc gaagagcgct 180 aagcctggca taatcattgc cagtccgagc accagcgaac cagactgtga gaaccttcct 240 gaactggccc tgtccggcag tcattgacct cggtagacta ctatacctgg acgagagatg 300 ctgctctcgt cacgaaagtc ctggtcgacc tcttccgcaa cggcaacctg ggtctgcaga 360 aagtcattac cgaatacgtc aactctcagg cgtacttgca gaccgtgtct aatccgtcgg 420 gtggtcttgc gagcggaggt ctcgcggagc ctaagtacaa cgtcgacatg acggccttta 480 ccggagcctg gggtcgtcct cagcgtgatg gtccggctct gcgggccacc gccctcatcg 540 actttggcaa ctggctgatt gtatgttctc catacgagcc ccaggaagcg ttgctgacgt 600 ctacaggaca acggctactc cagctatgct gtcaacaaca tctggcccat tgtgcgcaac 660 gacttgtcct acgtttctca gtactggagc cagagtggct ttggtgagtc ccgactctct 720 ggaagtttac aacgtgcatc gattactgac aattgagatt ctacgtgaca gatctctggg 780 aagaagtcaa ctccatgtcc ttcttcaccg tcgctgtcca gcaccgtgcc ctcgtggagg 840 gaagcacgtt cgctaaacgg gtgggagcgt cgtgctcgtg gtgtgactcg caggcccccc 900 agatcctctg ctacatgcag agtttctgga ctggctcgta tatcaacgcc aacaccggtg 960 gtggccggtc cggcaaggat gccaacaccg tcctcgccag catccatacc ttcgaccccg 1020 aagccggctg cgacgatact actttccagc cctgctctcc tcgggccctt gccaaccaca 1080 aggtgtacac cgattcgttc cgctcggtct acgcgatcaa ctccggcatc ccacagggcg 1140 ctgccgtttc cgctggccgc taccccgagg acgtctacta caacggcaac ccttggttcc 1200 tcaccaccct cgccgctgcc gagcagctct acgacgctat ctaccagtgg aagaagatcg 1260 gttccatcag catcaccagc acctccctcg ccttcttcaa ggacatctac agctccgccg 1320 cggtcggcac ctacgcctct agcacctcca ccttcacgga catcatcaac gcggtcaaga 1380 cctacgcaga cggctacgtg agcatcgtcc aggcacacgc catgaacaac ggctcccttt 1440 cggagcaatt cgacaagtcc tctgggctgt ccctctccgc ccgcgatctg acctggtcct 1500 acgccgcttt cctcaccgcc aacatgcgtc gtaacggcgt ggtgcctgcc ccctggggcg 1560 ccgcctccgc caactccgtc ccctcgtctt gctccatggg ctcggccacg ggcacctaca 1620 gcaccgcgac agccacctcc tggcccagca cgctgaccag cggctcgcca ggcagcacca 1680 ccaccgtggg caccacgacc agtaccacct ctggcaccgc caccgagacc gcctgtgcga 1740 cccctaccgc cgtggccgtc acctttaacg agatcgccac caccacctac ggcgagaatg 1800 tttacattgt tgggtccatc tccgagctcg ggaactggga taccagcaaa gcagtggccc 1860 tgagtgcgtc caagtatacc tccagcaata acctctggta cgtgtccgtc accctgccgg 1920 ctggcacgac attcgagtac aagtatatcc gcaaggaaag cgatggctcg atcgtgtggg 1980 agagtgaccc caaccgctcg tatacggtgc cggcagcttg tggagtgtct actgcgaccg 2040 agaatgatac ttggcggtga 2060 53 1896 DNA Aspergillus CDS (1)...(1896) 53 atg cct cgc ctt tcc tac gcg ctc tgt gcg ctg tct ctc ggg cat gct 48 Met Pro Arg Leu Ser Tyr Ala Leu Cys Ala Leu Ser Leu Gly His Ala 1 5 10 15 gct att gca gct cct cag tta tcc gct cgt gct acc ggc agc ttg gac 96 Ala Ile Ala Ala Pro Gln Leu Ser Ala Arg Ala Thr Gly Ser Leu Asp 20 25 30 tcc tgg ttg ggt act gag acc acc gtt gcg ctc aat ggt att ctg gcc 144 Ser Trp Leu Gly Thr Glu Thr Thr Val Ala Leu Asn Gly Ile Leu Ala 35 40 45 aac atc ggt gcc gac ggt gct tat gcg aag agc gct aag cct ggc ata 192 Asn Ile Gly Ala Asp Gly Ala Tyr Ala Lys Ser Ala Lys Pro Gly Ile 50 55 60 atc att gcc agt ccg agc acc agc gaa cca gac tac tac tat acc tgg 240 Ile Ile Ala Ser Pro Ser Thr Ser Glu Pro Asp Tyr Tyr Tyr Thr Trp 65 70 75 80 acg aga gat gct gct ctc gtc acg aaa gtc ctg gtc gac ctc ttc cgc 288 Thr Arg Asp Ala Ala Leu Val Thr Lys Val Leu Val Asp Leu Phe Arg 85 90 95 aac ggc aac ctg ggt ctg cag aaa gtc att acc gaa tac gtc aac tct 336 Asn Gly Asn Leu Gly Leu Gln Lys Val Ile Thr Glu Tyr Val Asn Ser 100 105 110 cag gcg tac ttg cag acc gtg tct aat ccg tcg ggt ggt ctt gcg agc 384 Gln Ala Tyr Leu Gln Thr Val Ser Asn Pro Ser Gly Gly Leu Ala Ser 115 120 125 gga ggt ctc gcg gag cct aag tac aac gtc gac atg acg gcc ttt acc 432 Gly Gly Leu Ala Glu Pro Lys Tyr Asn Val Asp Met Thr Ala Phe Thr 130 135 140 gga gcc tgg ggt cgt cct cag cgt gat ggt ccg gct ctg cgg gcc acc 480 Gly Ala Trp Gly Arg Pro Gln Arg Asp Gly Pro Ala Leu Arg Ala Thr 145 150 155 160 gcc ctc atc gac ttt ggc aac tgg ctg att gac aac ggc tac tcc agc 528 Ala Leu Ile Asp Phe Gly Asn Trp Leu Ile Asp Asn Gly Tyr Ser Ser 165 170 175 tat gct gtc aac aac atc tgg ccc att gtg cgc aac gac ttg tcc tac 576 Tyr Ala Val Asn Asn Ile Trp Pro Ile Val Arg Asn Asp Leu Ser Tyr 180 185 190 gtt tct cag tac tgg agc cag agt ggc ttt gat ctc tgg gaa gaa gtc 624 Val Ser Gln Tyr Trp Ser Gln Ser Gly Phe Asp Leu Trp Glu Glu Val 195 200 205 aac tcc atg tcc ttc ttc acc gtc gct gtc cag cac cgt gcc ctc gtg 672 Asn Ser Met Ser Phe Phe Thr Val Ala Val Gln His Arg Ala Leu Val 210 215 220 gag gga agc acg ttc gct aaa cgg gtg gga gcg tcg tgc tcg tgg tgt 720 Glu Gly Ser Thr Phe Ala Lys Arg Val Gly Ala Ser Cys Ser Trp Cys 225 230 235 240 gac tcg cag gcc ccc cag atc ctc tgc tac atg cag agt ttc tgg act 768 Asp Ser Gln Ala Pro Gln Ile Leu Cys Tyr Met Gln Ser Phe Trp Thr 245 250 255 ggc tcg tat atc aac gcc aac acc ggt ggt ggc cgg tcc ggc aag gat 816 Gly Ser Tyr Ile Asn Ala Asn Thr Gly Gly Gly Arg Ser Gly Lys Asp 260 265 270 gcc aac acc gtc ctc gcc agc atc cat acc ttc gac ccc gaa gcc ggc 864 Ala Asn Thr Val Leu Ala Ser Ile His Thr Phe Asp Pro Glu Ala Gly 275 280 285 tgc gac gat act act ttc cag ccc tgc tct cct cgg gcc ctt gcc aac 912 Cys Asp Asp Thr Thr Phe Gln Pro Cys Ser Pro Arg Ala Leu Ala Asn 290 295 300 cac aag gtg tac acc gat tcg ttc cgc tcg gtc tac gcg atc aac tcc 960 His Lys Val Tyr Thr Asp Ser Phe Arg Ser Val Tyr Ala Ile Asn Ser 305 310 315 320 ggc atc cca cag ggc gct gcc gtt tcc gct ggc cgc tac ccc gag gac 1008 Gly Ile Pro Gln Gly Ala Ala Val Ser Ala Gly Arg Tyr Pro Glu Asp 325 330 335 gtc tac tac aac ggc aac cct tgg ttc ctc acc acc ctc gcc gct gcc 1056 Val Tyr Tyr Asn Gly Asn Pro Trp Phe Leu Thr Thr Leu Ala Ala Ala 340 345 350 gag cag ctc tac gac gct atc tac cag tgg aag aag atc ggt tcc atc 1104 Glu Gln Leu Tyr Asp Ala Ile Tyr Gln Trp Lys Lys Ile Gly Ser Ile 355 360 365 agc atc acc agc acc tcc ctc gcc ttc ttc aag gac atc tac agc tcc 1152 Ser Ile Thr Ser Thr Ser Leu Ala Phe Phe Lys Asp Ile Tyr Ser Ser 370 375 380 gcc gcg gtc ggc acc tac gcc tct agc acc tcc acc ttc acg gac atc 1200 Ala Ala Val Gly Thr Tyr Ala Ser Ser Thr Ser Thr Phe Thr Asp Ile 385 390 395 400 atc aac gcg gtc aag acc tac gca gac ggc tac gtg agc atc gtc cag 1248 Ile Asn Ala Val Lys Thr Tyr Ala Asp Gly Tyr Val Ser Ile Val Gln 405 410 415 gca cac gcc atg aac aac ggc tcc ctt tcg gag caa ttc gac aag tcc 1296 Ala His Ala Met Asn Asn Gly Ser Leu Ser Glu Gln Phe Asp Lys Ser 420 425 430 tct ggg ctg tcc ctc tcc gcc cgc gat ctg acc tgg tcc tac gcc gct 1344 Ser Gly Leu Ser Leu Ser Ala Arg Asp Leu Thr Trp Ser Tyr Ala Ala 435 440 445 ttc ctc acc gcc aac atg cgt cgt aac ggc gtg gtg cct gcc ccc tgg 1392 Phe Leu Thr Ala Asn Met Arg Arg Asn Gly Val Val Pro Ala Pro Trp 450 455 460 ggc gcc gcc tcc gcc aac tcc gtc ccc tcg tct tgc tcc atg ggc tcg 1440 Gly Ala Ala Ser Ala Asn Ser Val Pro Ser Ser Cys Ser Met Gly Ser 465 470 475 480 gcc acg ggc acc tac agc acc gcg aca gcc acc tcc tgg ccc agc acg 1488 Ala Thr Gly Thr Tyr Ser Thr Ala Thr Ala Thr Ser Trp Pro Ser Thr 485 490 495 ctg acc agc ggc tcg cca ggc agc acc acc acc gtg ggc acc acg acc 1536 Leu Thr Ser Gly Ser Pro Gly Ser Thr Thr Thr Val Gly Thr Thr Thr 500 505 510 agt acc acc tct ggc acc gcc acc gag acc gcc tgt gcg acc cct acc 1584 Ser Thr Thr Ser Gly Thr Ala Thr Glu Thr Ala Cys Ala Thr Pro Thr 515 520 525 gcc gtg gcc gtc acc ttt aac gag atc gcc acc acc acc tac ggc gag 1632 Ala Val Ala Val Thr Phe Asn Glu Ile Ala Thr Thr Thr Tyr Gly Glu 530 535 540 aat gtt tac att gtt ggg tcc atc tcc gag ctc ggg aac tgg gat acc 1680 Asn Val Tyr Ile Val Gly Ser Ile Ser Glu Leu Gly Asn Trp Asp Thr 545 550 555 560 agc aaa gca gtg gcc ctg agt gcg tcc aag tat acc tcc agc aat aac 1728 Ser Lys Ala Val Ala Leu Ser Ala Ser Lys Tyr Thr Ser Ser Asn Asn 565 570 575 ctc tgg tac gtg tcc gtc acc ctg ccg gct ggc acg aca ttc gag tac 1776 Leu Trp Tyr Val Ser Val Thr Leu Pro Ala Gly Thr Thr Phe Glu Tyr 580 585 590 aag tat atc cgc aag gaa agc gat ggc tcg atc gtg tgg gag agt gac 1824 Lys Tyr Ile Arg Lys Glu Ser Asp Gly Ser Ile Val Trp Glu Ser Asp 595 600 605 ccc aac cgc tcg tat acg gtg ccg gca gct tgt gga gtg tct act gcg 1872 Pro Asn Arg Ser Tyr Thr Val Pro Ala Ala Cys Gly Val Ser Thr Ala 610 615 620 acc gag aat gat act tgg cgg tga 1896 Thr Glu Asn Asp Thr Trp Arg * 625 630 54 631 PRT Aspergillus 54 Met Pro Arg Leu Ser Tyr Ala Leu Cys Ala Leu Ser Leu Gly His Ala 1 5 10 15 Ala Ile Ala Ala Pro Gln Leu Ser Ala Arg Ala Thr Gly Ser Leu Asp 20 25 30 Ser Trp Leu Gly Thr Glu Thr Thr Val Ala Leu Asn Gly Ile Leu Ala 35 40 45 Asn Ile Gly Ala Asp Gly Ala Tyr Ala Lys Ser Ala Lys Pro Gly Ile 50 55 60 Ile Ile Ala Ser Pro Ser Thr Ser Glu Pro Asp Tyr Tyr Tyr Thr Trp 65 70 75 80 Thr Arg Asp Ala Ala Leu Val Thr Lys Val Leu Val Asp Leu Phe Arg 85 90 95 Asn Gly Asn Leu Gly Leu Gln Lys Val Ile Thr Glu Tyr Val Asn Ser 100 105 110 Gln Ala Tyr Leu Gln Thr Val Ser Asn Pro Ser Gly Gly Leu Ala Ser 115 120 125 Gly Gly Leu Ala Glu Pro Lys Tyr Asn Val Asp Met Thr Ala Phe Thr 130 135 140 Gly Ala Trp Gly Arg Pro Gln Arg Asp Gly Pro Ala Leu Arg Ala Thr 145 150 155 160 Ala Leu Ile Asp Phe Gly Asn Trp Leu Ile Asp Asn Gly Tyr Ser Ser 165 170 175 Tyr Ala Val Asn Asn Ile Trp Pro Ile Val Arg Asn Asp Leu Ser Tyr 180 185 190 Val Ser Gln Tyr Trp Ser Gln Ser Gly Phe Asp Leu Trp Glu Glu Val 195 200 205 Asn Ser Met Ser Phe Phe Thr Val Ala Val Gln His Arg Ala Leu Val 210 215 220 Glu Gly Ser Thr Phe Ala Lys Arg Val Gly Ala Ser Cys Ser Trp Cys 225 230 235 240 Asp Ser Gln Ala Pro Gln Ile Leu Cys Tyr Met Gln Ser Phe Trp Thr 245 250 255 Gly Ser Tyr Ile Asn Ala Asn Thr Gly Gly Gly Arg Ser Gly Lys Asp 260 265 270 Ala Asn Thr Val Leu Ala Ser Ile His Thr Phe Asp Pro Glu Ala Gly 275 280 285 Cys Asp Asp Thr Thr Phe Gln Pro Cys Ser Pro Arg Ala Leu Ala Asn 290 295 300 His Lys Val Tyr Thr Asp Ser Phe Arg Ser Val Tyr Ala Ile Asn Ser 305 310 315 320 Gly Ile Pro Gln Gly Ala Ala Val Ser Ala Gly Arg Tyr Pro Glu Asp 325 330 335 Val Tyr Tyr Asn Gly Asn Pro Trp Phe Leu Thr Thr Leu Ala Ala Ala 340 345 350 Glu Gln Leu Tyr Asp Ala Ile Tyr Gln Trp Lys Lys Ile Gly Ser Ile 355 360 365 Ser Ile Thr Ser Thr Ser Leu Ala Phe Phe Lys Asp Ile Tyr Ser Ser 370 375 380 Ala Ala Val Gly Thr Tyr Ala Ser Ser Thr Ser Thr Phe Thr Asp Ile 385 390 395 400 Ile Asn Ala Val Lys Thr Tyr Ala Asp Gly Tyr Val Ser Ile Val Gln 405 410 415 Ala His Ala Met Asn Asn Gly Ser Leu Ser Glu Gln Phe Asp Lys Ser 420 425 430 Ser Gly Leu Ser Leu Ser Ala Arg Asp Leu Thr Trp Ser Tyr Ala Ala 435 440 445 Phe Leu Thr Ala Asn Met Arg Arg Asn Gly Val Val Pro Ala Pro Trp 450 455 460 Gly Ala Ala Ser Ala Asn Ser Val Pro Ser Ser Cys Ser Met Gly Ser 465 470 475 480 Ala Thr Gly Thr Tyr Ser Thr Ala Thr Ala Thr Ser Trp Pro Ser Thr 485 490 495 Leu Thr Ser Gly Ser Pro Gly Ser Thr Thr Thr Val Gly Thr Thr Thr 500 505 510 Ser Thr Thr Ser Gly Thr Ala Thr Glu Thr Ala Cys Ala Thr Pro Thr 515 520 525 Ala Val Ala Val Thr Phe Asn Glu Ile Ala Thr Thr Thr Tyr Gly Glu 530 535 540 Asn Val Tyr Ile Val Gly Ser Ile Ser Glu Leu Gly Asn Trp Asp Thr 545 550 555 560 Ser Lys Ala Val Ala Leu Ser Ala Ser Lys Tyr Thr Ser Ser Asn Asn 565 570 575 Leu Trp Tyr Val Ser Val Thr Leu Pro Ala Gly Thr Thr Phe Glu Tyr 580 585 590 Lys Tyr Ile Arg Lys Glu Ser Asp Gly Ser Ile Val Trp Glu Ser Asp 595 600 605 Pro Asn Arg Ser Tyr Thr Val Pro Ala Ala Cys Gly Val Ser Thr Ala 610 615 620 Thr Glu Asn Asp Thr Trp Arg 625 630 55 1316 DNA Aspergillus 55 atgctgaaac tgatgggttc tcttgttctc ctcgcgtctg cggccgaggt gattgcctct 60 cccgcggctg agccagttgc gccgtccaca actctggaga agcgcgcacc ttgcacgttt 120 tccgggtcca acggcgccgc tgctgcgatg gcttctcaga aggcttgctc cactattgtc 180 ctgtcaaacg tggctgttcc ggctggcacg acgctggacc ttagcgatct ggcggatggc 240 accacagtac gaaccccatc tccgacacca accccctaat tcgtcgaggc aatagtctaa 300 ttactccagg tcaccttcga gggcgagaca acctggggtt accaggagtg gtccggtcca 360 ctgctgaaga tttccggcaa gaacatcaag gtgaagggcg cgtcgggggc tacgctgaac 420 cccgacggcg cccgctggtg ggacggccag ggcggcaacg gcggcaagac gaagcccaag 480 ttcttcgccg cgcacgatct cacctcgtca tcatccatca ccgatctgca catcttgaac 540 acccccgtcc aggcggtcag catcaacgga tgcgatggcc tgaccatcac cgacataacg 600 atcgacaatt ccgccggaga cacccaaggc ggccacaaca ctgacgcctt cgatattgga 660 tccagctcca acattatcat ttcaggcgcc aaggtctaca accaggacga ctgtgtcgcg 720 gtcaactccg gcacggatat cacctttacc ggggggctct gctccggtgg ccatggcctg 780 tcgattggta gcgttggtgg ccggtctgat aatactgtcg agaatgtgtc ctttaccaac 840 tcccaggtga ccaactccga caatggtacc atcacctccc cccgttgtct tgtcgagggt 900 aaacttctaa ccatgaagca ggtctccgca tcaaggccac caaagggaag actggcacaa 960 tcaagggagt cacctactca ggcatcaccc tgagctccat ccgcaagtca gctctcctcg 1020 gcttcttcgt ataaaagatg acggttatca agctaacatt gccaaggtac ggtatcctca 1080 tcgagcaaaa ctacgacggc ggcgatctca agggcgaccc gacgtccggc atccccatca 1140 ccgacctcac catgcagaac atcagtggta aaggcgccgt ggcgtcaagc gggtacaata 1200 ttgctattgt ctgcggcagt ggggcttgct cgaactggac ctggaagagc gtcgaggtta 1260 ccggcgggaa gacctatggt agctgcaaga acgttcctag cgttgcccaa tgctag 1316 56 1137 DNA Aspergillus CDS (1)...(1137) 56 atg ctg aaa ctg atg ggt tct ctt gtt ctc ctc gcg tct gcg gcc gag 48 Met Leu Lys Leu Met Gly Ser Leu Val Leu Leu Ala Ser Ala Ala Glu 1 5 10 15 gtg att gcc tct ccc gcg gct gag cca gtt gcg ccg tcc aca act ctg 96 Val Ile Ala Ser Pro Ala Ala Glu Pro Val Ala Pro Ser Thr Thr Leu 20 25 30 gag aag cgc gca cct tgc acg ttt tcc ggg tcc aac ggc gcc gct gct 144 Glu Lys Arg Ala Pro Cys Thr Phe Ser Gly Ser Asn Gly Ala Ala Ala 35 40 45 gcg atg gct tct cag aag gct tgc tcc act att gtc ctg tca aac gtg 192 Ala Met Ala Ser Gln Lys Ala Cys Ser Thr Ile Val Leu Ser Asn Val 50 55 60 gct gtt ccg gct ggc acg acg ctg gac ctt agc gat ctg gcg gat ggc 240 Ala Val Pro Ala Gly Thr Thr Leu Asp Leu Ser Asp Leu Ala Asp Gly 65 70 75 80 acc aca gtc acc ttc gag ggc gag aca acc tgg ggt tac cag gag tgg 288 Thr Thr Val Thr Phe Glu Gly Glu Thr Thr Trp Gly Tyr Gln Glu Trp 85 90 95 tcc ggt cca ctg ctg aag att tcc ggc aag aac atc aag gtg aag ggc 336 Ser Gly Pro Leu Leu Lys Ile Ser Gly Lys Asn Ile Lys Val Lys Gly 100 105 110 gcg tcg ggg gct acg ctg aac ccc gac ggc gcc cgc tgg tgg gac ggc 384 Ala Ser Gly Ala Thr Leu Asn Pro Asp Gly Ala Arg Trp Trp Asp Gly 115 120 125 cag ggc ggc aac ggc ggc aag acg aag ccc aag ttc ttc gcc gcg cac 432 Gln Gly Gly Asn Gly Gly Lys Thr Lys Pro Lys Phe Phe Ala Ala His 130 135 140 gat ctc acc tcg tca tca tcc atc acc gat ctg cac atc ttg aac acc 480 Asp Leu Thr Ser Ser Ser Ser Ile Thr Asp Leu His Ile Leu Asn Thr 145 150 155 160 ccc gtc cag gcg gtc agc atc aac gga tgc gat ggc ctg acc atc acc 528 Pro Val Gln Ala Val Ser Ile Asn Gly Cys Asp Gly Leu Thr Ile Thr 165 170 175 gac ata acg atc gac aat tcc gcc gga gac acc caa ggc ggc cac aac 576 Asp Ile Thr Ile Asp Asn Ser Ala Gly Asp Thr Gln Gly Gly His Asn 180 185 190 act gac gcc ttc gat att gga tcc agc tcc aac att atc att tca ggc 624 Thr Asp Ala Phe Asp Ile Gly Ser Ser Ser Asn Ile Ile Ile Ser Gly 195 200 205 gcc aag gtc tac aac cag gac gac tgt gtc gcg gtc aac tcc ggc acg 672 Ala Lys Val Tyr Asn Gln Asp Asp Cys Val Ala Val Asn Ser Gly Thr 210 215 220 gat atc acc ttt acc ggg ggg ctc tgc tcc ggt ggc cat ggc ctg tcg 720 Asp Ile Thr Phe Thr Gly Gly Leu Cys Ser Gly Gly His Gly Leu Ser 225 230 235 240 att ggt agc gtt ggt ggc cgg tct gat aat act gtc gag aat gtg tcc 768 Ile Gly Ser Val Gly Gly Arg Ser Asp Asn Thr Val Glu Asn Val Ser 245 250 255 ttt acc aac tcc cag gtg acc aac tcc gac aat ggt ctc cgc atc aag 816 Phe Thr Asn Ser Gln Val Thr Asn Ser Asp Asn Gly Leu Arg Ile Lys 260 265 270 gcc acc aaa ggg aag act ggc aca atc aag gga gtc acc tac tca ggc 864 Ala Thr Lys Gly Lys Thr Gly Thr Ile Lys Gly Val Thr Tyr Ser Gly 275 280 285 atc acc ctg agc tcc atc cgc aag tac ggt atc ctc atc gag caa aac 912 Ile Thr Leu Ser Ser Ile Arg Lys Tyr Gly Ile Leu Ile Glu Gln Asn 290 295 300 tac gac ggc ggc gat ctc aag ggc gac ccg acg tcc ggc atc ccc atc 960 Tyr Asp Gly Gly Asp Leu Lys Gly Asp Pro Thr Ser Gly Ile Pro Ile 305 310 315 320 acc gac ctc acc atg cag aac atc agt ggt aaa ggc gcc gtg gcg tca 1008 Thr Asp Leu Thr Met Gln Asn Ile Ser Gly Lys Gly Ala Val Ala Ser 325 330 335 agc ggg tac aat att gct att gtc tgc ggc agt ggg gct tgc tcg aac 1056 Ser Gly Tyr Asn Ile Ala Ile Val Cys Gly Ser Gly Ala Cys Ser Asn 340 345 350 tgg acc tgg aag agc gtc gag gtt acc ggc ggg aag acc tat ggt agc 1104 Trp Thr Trp Lys Ser Val Glu Val Thr Gly Gly Lys Thr Tyr Gly Ser 355 360 365 tgc aag aac gtt cct agc gtt gcc caa tgc tag 1137 Cys Lys Asn Val Pro Ser Val Ala Gln Cys * 370 375 57 378 PRT Aspergillus 57 Met Leu Lys Leu Met Gly Ser Leu Val Leu Leu Ala Ser Ala Ala Glu 1 5 10 15 Val Ile Ala Ser Pro Ala Ala Glu Pro Val Ala Pro Ser Thr Thr Leu 20 25 30 Glu Lys Arg Ala Pro Cys Thr Phe Ser Gly Ser Asn Gly Ala Ala Ala 35 40 45 Ala Met Ala Ser Gln Lys Ala Cys Ser Thr Ile Val Leu Ser Asn Val 50 55 60 Ala Val Pro Ala Gly Thr Thr Leu Asp Leu Ser Asp Leu Ala Asp Gly 65 70 75 80 Thr Thr Val Thr Phe Glu Gly Glu Thr Thr Trp Gly Tyr Gln Glu Trp 85 90 95 Ser Gly Pro Leu Leu Lys Ile Ser Gly Lys Asn Ile Lys Val Lys Gly 100 105 110 Ala Ser Gly Ala Thr Leu Asn Pro Asp Gly Ala Arg Trp Trp Asp Gly 115 120 125 Gln Gly Gly Asn Gly Gly Lys Thr Lys Pro Lys Phe Phe Ala Ala His 130 135 140 Asp Leu Thr Ser Ser Ser Ser Ile Thr Asp Leu His Ile Leu Asn Thr 145 150 155 160 Pro Val Gln Ala Val Ser Ile Asn Gly Cys Asp Gly Leu Thr Ile Thr 165 170 175 Asp Ile Thr Ile Asp Asn Ser Ala Gly Asp Thr Gln Gly Gly His Asn 180 185 190 Thr Asp Ala Phe Asp Ile Gly Ser Ser Ser Asn Ile Ile Ile Ser Gly 195 200 205 Ala Lys Val Tyr Asn Gln Asp Asp Cys Val Ala Val Asn Ser Gly Thr 210 215 220 Asp Ile Thr Phe Thr Gly Gly Leu Cys Ser Gly Gly His Gly Leu Ser 225 230 235 240 Ile Gly Ser Val Gly Gly Arg Ser Asp Asn Thr Val Glu Asn Val Ser 245 250 255 Phe Thr Asn Ser Gln Val Thr Asn Ser Asp Asn Gly Leu Arg Ile Lys 260 265 270 Ala Thr Lys Gly Lys Thr Gly Thr Ile Lys Gly Val Thr Tyr Ser Gly 275 280 285 Ile Thr Leu Ser Ser Ile Arg Lys Tyr Gly Ile Leu Ile Glu Gln Asn 290 295 300 Tyr Asp Gly Gly Asp Leu Lys Gly Asp Pro Thr Ser Gly Ile Pro Ile 305 310 315 320 Thr Asp Leu Thr Met Gln Asn Ile Ser Gly Lys Gly Ala Val Ala Ser 325 330 335 Ser Gly Tyr Asn Ile Ala Ile Val Cys Gly Ser Gly Ala Cys Ser Asn 340 345 350 Trp Thr Trp Lys Ser Val Glu Val Thr Gly Gly Lys Thr Tyr Gly Ser 355 360 365 Cys Lys Asn Val Pro Ser Val Ala Gln Cys 370 375 58 1238 DNA Aspergillus 58 atgcgttctg ttaagctttt tggcctggct gcgctgggct ccctcggcgc tgctgcccct 60 gctccgtctc gcgtgtcgga tctgaccaag aggtcttcaa cttgtacctt caccgcagcc 120 tcccaggcta ccgagagcgc ttctggttgc tccgagattg tcctggacaa catcgaggtt 180 cctgccggtg agacactgga tctctcggat gttgatgatg gaaccaccgt acgttaatac 240 cattgattat ctccctgtct atctctctgc cattgctccc gagctaatcc ccgaagatcg 300 tcttcgaagg caccaccacc tttggctata aagagtggag cggccccttg atccgcttcg 360 gcggcaagga catcaccatc aagcagaact ccggcgctgt gattgacgga gaaggctccc 420 gctggtggga cggcgagggc accaatggcg gcaagaccaa gcccaagttc atgtacgcgc 480 acagcctcga ggactcgacc atcaccgggc tatccatcaa gaacacacct gtgcaggcca 540 ttagtgttca ggcgaccaac ctctacctga tcgacatcac catcgataac tccgacgggg 600 atgacaacgg cgggcacaac actgacgggt ttgacatcag cgagagtacc ggggtgtata 660 tccgcggcgc taccgtcaag aaccaggatg actgcattgc catcaactcc ggcgaggtat 720 gctcccctgt cttttttttt ttttccccgc aggttggcat tgaagttaat tgactccaga 780 acatcgaatt ctccggtggt acctgctctg gcggccacgg tctctccatt ggctcggttg 840 gcggtcgcga cgacaacacc gtcaagaacg tcaccatcac cgactccacc gtgaccgatt 900 cggccaacgg cgtgcgtatc aagacggtct acgacgccac cggctctgtt agccaagtca 960 cctactccaa catcaagctg tcaggtatca cggactatgg tatcgtcatc gagcaggact 1020 acgagaacgg cagcccgacc ggtaccccta ccactggcgt tccgatcacc gacctgacta 1080 tcgacggtgt gactggtacc gtcgagtccg acgccgtcga ggtgtacatt ctttgcggag 1140 acggtagctg cagtgactgg acctgggagg gcgtggatat cactggcggg gagaagagct 1200 ccaagtgcga gaatgttccc tcaggtgctt cttgctag 1238 59 1107 DNA Aspergillus CDS (1)...(1107) 59 atg cgt tct gtt aag ctt ttt ggc ctg gct gcg ctg ggc tcc ctc ggc 48 Met Arg Ser Val Lys Leu Phe Gly Leu Ala Ala Leu Gly Ser Leu Gly 1 5 10 15 gct gct gcc cct gct ccg tct cgc gtg tcg gat ctg acc aag agg tct 96 Ala Ala Ala Pro Ala Pro Ser Arg Val Ser Asp Leu Thr Lys Arg Ser 20 25 30 tca act tgt acc ttc acc gca gcc tcc cag gct acc gag agc gct tct 144 Ser Thr Cys Thr Phe Thr Ala Ala Ser Gln Ala Thr Glu Ser Ala Ser 35 40 45 ggt tgc tcc gag att gtc ctg gac aac atc gag gtt cct gcc ggt gag 192 Gly Cys Ser Glu Ile Val Leu Asp Asn Ile Glu Val Pro Ala Gly Glu 50 55 60 aca ctg gat ctc tcg gat gtt gat gat gga acc acc atc gtc ttc gaa 240 Thr Leu Asp Leu Ser Asp Val Asp Asp Gly Thr Thr Ile Val Phe Glu 65 70 75 80 ggc acc acc acc ttt ggc tat aaa gag tgg agc ggc ccc ttg atc cgc 288 Gly Thr Thr Thr Phe Gly Tyr Lys Glu Trp Ser Gly Pro Leu Ile Arg 85 90 95 ttc ggc ggc aag gac atc acc atc aag cag aac tcc ggc gct gtg att 336 Phe Gly Gly Lys Asp Ile Thr Ile Lys Gln Asn Ser Gly Ala Val Ile 100 105 110 gac gga gaa ggc tcc cgc tgg tgg gac ggc gag ggc acc aat ggc ggc 384 Asp Gly Glu Gly Ser Arg Trp Trp Asp Gly Glu Gly Thr Asn Gly Gly 115 120 125 aag acc aag ccc aag ttc atg tac gcg cac agc ctc gag gac tcg acc 432 Lys Thr Lys Pro Lys Phe Met Tyr Ala His Ser Leu Glu Asp Ser Thr 130 135 140 atc acc ggg cta tcc atc aag aac aca cct gtg cag gcc att agt gtt 480 Ile Thr Gly Leu Ser Ile Lys Asn Thr Pro Val Gln Ala Ile Ser Val 145 150 155 160 cag gcg acc aac ctc tac ctg atc gac atc acc atc gat aac tcc gac 528 Gln Ala Thr Asn Leu Tyr Leu Ile Asp Ile Thr Ile Asp Asn Ser Asp 165 170 175 ggg gat gac aac ggc ggg cac aac act gac ggg ttt gac atc agc gag 576 Gly Asp Asp Asn Gly Gly His Asn Thr Asp Gly Phe Asp Ile Ser Glu 180 185 190 agt acc ggg gtg tat atc cgc ggc gct acc gtc aag aac cag gat gac 624 Ser Thr Gly Val Tyr Ile Arg Gly Ala Thr Val Lys Asn Gln Asp Asp 195 200 205 tgc att gcc atc aac tcc ggc gag aac atc gaa ttc tcc ggt ggt acc 672 Cys Ile Ala Ile Asn Ser Gly Glu Asn Ile Glu Phe Ser Gly Gly Thr 210 215 220 tgc tct ggc ggc cac ggt ctc tcc att ggc tcg gtt ggc ggt cgc gac 720 Cys Ser Gly Gly His Gly Leu Ser Ile Gly Ser Val Gly Gly Arg Asp 225 230 235 240 gac aac acc gtc aag aac gtc acc atc acc gac tcc acc gtg acc gat 768 Asp Asn Thr Val Lys Asn Val Thr Ile Thr Asp Ser Thr Val Thr Asp 245 250 255 tcg gcc aac ggc gtg cgt atc aag acg gtc tac gac gcc acc ggc tct 816 Ser Ala Asn Gly Val Arg Ile Lys Thr Val Tyr Asp Ala Thr Gly Ser 260 265 270 gtt agc caa gtc acc tac tcc aac atc aag ctg tca ggt atc acg gac 864 Val Ser Gln Val Thr Tyr Ser Asn Ile Lys Leu Ser Gly Ile Thr Asp 275 280 285 tat ggt atc gtc atc gag cag gac tac gag aac ggc agc ccg acc ggt 912 Tyr Gly Ile Val Ile Glu Gln Asp Tyr Glu Asn Gly Ser Pro Thr Gly 290 295 300 acc cct acc act ggc gtt ccg atc acc gac ctg act atc gac ggt gtg 960 Thr Pro Thr Thr Gly Val Pro Ile Thr Asp Leu Thr Ile Asp Gly Val 305 310 315 320 act ggt acc gtc gag tcc gac gcc gtc gag gtg tac att ctt tgc gga 1008 Thr Gly Thr Val Glu Ser Asp Ala Val Glu Val Tyr Ile Leu Cys Gly 325 330 335 gac ggt agc tgc agt gac tgg acc tgg gag ggc gtg gat atc act ggc 1056 Asp Gly Ser Cys Ser Asp Trp Thr Trp Glu Gly Val Asp Ile Thr Gly 340 345 350 ggg gag aag agc tcc aag tgc gag aat gtt ccc tca ggt gct tct tgc 1104 Gly Glu Lys Ser Ser Lys Cys Glu Asn Val Pro Ser Gly Ala Ser Cys 355 360 365 tag 1107 * 60 368 PRT Aspergillus 60 Met Arg Ser Val Lys Leu Phe Gly Leu Ala Ala Leu Gly Ser Leu Gly 1 5 10 15 Ala Ala Ala Pro Ala Pro Ser Arg Val Ser Asp Leu Thr Lys Arg Ser 20 25 30 Ser Thr Cys Thr Phe Thr Ala Ala Ser Gln Ala Thr Glu Ser Ala Ser 35 40 45 Gly Cys Ser Glu Ile Val Leu Asp Asn Ile Glu Val Pro Ala Gly Glu 50 55 60 Thr Leu Asp Leu Ser Asp Val Asp Asp Gly Thr Thr Ile Val Phe Glu 65 70 75 80 Gly Thr Thr Thr Phe Gly Tyr Lys Glu Trp Ser Gly Pro Leu Ile Arg 85 90 95 Phe Gly Gly Lys Asp Ile Thr Ile Lys Gln Asn Ser Gly Ala Val Ile 100 105 110 Asp Gly Glu Gly Ser Arg Trp Trp Asp Gly Glu Gly Thr Asn Gly Gly 115 120 125 Lys Thr Lys Pro Lys Phe Met Tyr Ala His Ser Leu Glu Asp Ser Thr 130 135 140 Ile Thr Gly Leu Ser Ile Lys Asn Thr Pro Val Gln Ala Ile Ser Val 145 150 155 160 Gln Ala Thr Asn Leu Tyr Leu Ile Asp Ile Thr Ile Asp Asn Ser Asp 165 170 175 Gly Asp Asp Asn Gly Gly His Asn Thr Asp Gly Phe Asp Ile Ser Glu 180 185 190 Ser Thr Gly Val Tyr Ile Arg Gly Ala Thr Val Lys Asn Gln Asp Asp 195 200 205 Cys Ile Ala Ile Asn Ser Gly Glu Asn Ile Glu Phe Ser Gly Gly Thr 210 215 220 Cys Ser Gly Gly His Gly Leu Ser Ile Gly Ser Val Gly Gly Arg Asp 225 230 235 240 Asp Asn Thr Val Lys Asn Val Thr Ile Thr Asp Ser Thr Val Thr Asp 245 250 255 Ser Ala Asn Gly Val Arg Ile Lys Thr Val Tyr Asp Ala Thr Gly Ser 260 265 270 Val Ser Gln Val Thr Tyr Ser Asn Ile Lys Leu Ser Gly Ile Thr Asp 275 280 285 Tyr Gly Ile Val Ile Glu Gln Asp Tyr Glu Asn Gly Ser Pro Thr Gly 290 295 300 Thr Pro Thr Thr Gly Val Pro Ile Thr Asp Leu Thr Ile Asp Gly Val 305 310 315 320 Thr Gly Thr Val Glu Ser Asp Ala Val Glu Val Tyr Ile Leu Cys Gly 325 330 335 Asp Gly Ser Cys Ser Asp Trp Thr Trp Glu Gly Val Asp Ile Thr Gly 340 345 350 Gly Glu Lys Ser Ser Lys Cys Glu Asn Val Pro Ser Gly Ala Ser Cys 355 360 365 61 1149 DNA Aspergillus 61 atgcatttct tccaatcctc cctcgtggcc gcgaccatgg gcgctgcgct ggtcgctgcc 60 gcacctgccg ctgatctcga gactcgcggc tcttgcactt tcacctctac gtccgcgctc 120 aagtccggca aggcctcgtg ctccaccatc actctccaga acatcgcggt gcccgcgggt 180 gagaccctgg acctgactgg cctgaaggcc ggtaccactg taagtcttac ccttgaattg 240 tctgaatgcc atcggctgat gtgctgccaa aaggtcgtct tcgacggtac caccaccttc 300 ggctacaagg aatgggaggg ccccctgatt tccgcgtccg gaaccagtat taccatcaag 360 cagaaccctg gtgctaagat tgactgtgat ggtgctcgtt ggtgggacgg caagggaggc 420 aacggtggca agaagaagcc caagttcttc tctgcccaca agctgaacaa gtcgaacatc 480 accggcctga aggtctacaa cacccccgtc catggcttca gcatccagtc cgaccacctc 540 accatcaagg acgtcctcct cgacaactcc gccggtacca agctcggcca caataccgat 600 gcctttgacg tcggttccag cacctacatc actattgacg gcgccaccgt ctacaaccag 660 gacgactgcc tggccgtcaa ctccggtgag cacatcacct tcaccaacgg ctactgcaac 720 ggtggtcacg gtctctccat cggctccgtc ggcggccgca gtaacaatgt cgtcaacgac 780 gtcaccatct ccaactccca ggtcatcaac tcccagaacg gtgctcggat caagaccgtc 840 tacggcgcga ctggctctgt caccggcgtc aagttccagg atatctccct caaaggtatc 900 accaagtacg gtattgttgt ccagcaggac tacgagaacg gcaagcccac tggcaagccc 960 accaacggcg tcaaggtctc cgatatcacc ttcgagaagg tcaccggtac cgtcaccagc 1020 tccgccactg atatttacat tctctgcgga tctggcagct gcaccaactg gacctggtct 1080 ggcaatagcg tcaccggtgg caagaagagc tccagttgca agaacgttcc tgctggcgcc 1140 tcatgctag 1149 62 1095 DNA Aspergillus CDS (1)...(1095) 62 atg cat ttc ttc caa tcc tcc ctc gtg gcc gcg acc atg ggc gct gcg 48 Met His Phe Phe Gln Ser Ser Leu Val Ala Ala Thr Met Gly Ala Ala 1 5 10 15 ctg gtc gct gcc gca cct gcc gct gat ctc gag act cgc ggc tct tgc 96 Leu Val Ala Ala Ala Pro Ala Ala Asp Leu Glu Thr Arg Gly Ser Cys 20 25 30 act ttc acc tct acg tcc gcg ctc aag tcc ggc aag gcc tcg tgc tcc 144 Thr Phe Thr Ser Thr Ser Ala Leu Lys Ser Gly Lys Ala Ser Cys Ser 35 40 45 acc atc act ctc cag aac atc gcg gtg ccc gcg ggt gag acc ctg gac 192 Thr Ile Thr Leu Gln Asn Ile Ala Val Pro Ala Gly Glu Thr Leu Asp 50 55 60 ctg act ggc ctg aag gcc ggt acc act gtc gtc ttc gac ggt acc acc 240 Leu Thr Gly Leu Lys Ala Gly Thr Thr Val Val Phe Asp Gly Thr Thr 65 70 75 80 acc ttc ggc tac aag gaa tgg gag ggc ccc ctg att tcc gcg tcc gga 288 Thr Phe Gly Tyr Lys Glu Trp Glu Gly Pro Leu Ile Ser Ala Ser Gly 85 90 95 acc agt att acc atc aag cag aac cct ggt gct aag att gac tgt gat 336 Thr Ser Ile Thr Ile Lys Gln Asn Pro Gly Ala Lys Ile Asp Cys Asp 100 105 110 ggt gct cgt tgg tgg gac ggc aag gga ggc aac ggt ggc aag aag aag 384 Gly Ala Arg Trp Trp Asp Gly Lys Gly Gly Asn Gly Gly Lys Lys Lys 115 120 125 ccc aag ttc ttc tct gcc cac aag ctg aac aag tcg aac atc acc ggc 432 Pro Lys Phe Phe Ser Ala His Lys Leu Asn Lys Ser Asn Ile Thr Gly 130 135 140 ctg aag gtc tac aac acc ccc gtc cat ggc ttc agc atc cag tcc gac 480 Leu Lys Val Tyr Asn Thr Pro Val His Gly Phe Ser Ile Gln Ser Asp 145 150 155 160 cac ctc acc atc aag gac gtc ctc ctc gac aac tcc gcc ggt acc aag 528 His Leu Thr Ile Lys Asp Val Leu Leu Asp Asn Ser Ala Gly Thr Lys 165 170 175 ctc ggc cac aat acc gat gcc ttt gac gtc ggt tcc agc acc tac atc 576 Leu Gly His Asn Thr Asp Ala Phe Asp Val Gly Ser Ser Thr Tyr Ile 180 185 190 act att gac ggc gcc acc gtc tac aac cag gac gac tgc ctg gcc gtc 624 Thr Ile Asp Gly Ala Thr Val Tyr Asn Gln Asp Asp Cys Leu Ala Val 195 200 205 aac tcc ggt gag cac atc acc ttc acc aac ggc tac tgc aac ggt ggt 672 Asn Ser Gly Glu His Ile Thr Phe Thr Asn Gly Tyr Cys Asn Gly Gly 210 215 220 cac ggt ctc tcc atc ggc tcc gtc ggc ggc cgc agt aac aat gtc gtc 720 His Gly Leu Ser Ile Gly Ser Val Gly Gly Arg Ser Asn Asn Val Val 225 230 235 240 aac gac gtc acc atc tcc aac tcc cag gtc atc aac tcc cag aac ggt 768 Asn Asp Val Thr Ile Ser Asn Ser Gln Val Ile Asn Ser Gln Asn Gly 245 250 255 gct cgg atc aag acc gtc tac ggc gcg act ggc tct gtc acc ggc gtc 816 Ala Arg Ile Lys Thr Val Tyr Gly Ala Thr Gly Ser Val Thr Gly Val 260 265 270 aag ttc cag gat atc tcc ctc aaa ggt atc acc aag tac ggt att gtt 864 Lys Phe Gln Asp Ile Ser Leu Lys Gly Ile Thr Lys Tyr Gly Ile Val 275 280 285 gtc cag cag gac tac gag aac ggc aag ccc act ggc aag ccc acc aac 912 Val Gln Gln Asp Tyr Glu Asn Gly Lys Pro Thr Gly Lys Pro Thr Asn 290 295 300 ggc gtc aag gtc tcc gat atc acc ttc gag aag gtc acc ggt acc gtc 960 Gly Val Lys Val Ser Asp Ile Thr Phe Glu Lys Val Thr Gly Thr Val 305 310 315 320 acc agc tcc gcc act gat att tac att ctc tgc gga tct ggc agc tgc 1008 Thr Ser Ser Ala Thr Asp Ile Tyr Ile Leu Cys Gly Ser Gly Ser Cys 325 330 335 acc aac tgg acc tgg tct ggc aat agc gtc acc ggt ggc aag aag agc 1056 Thr Asn Trp Thr Trp Ser Gly Asn Ser Val Thr Gly Gly Lys Lys Ser 340 345 350 tcc agt tgc aag aac gtt cct gct ggc gcc tca tgc tag 1095 Ser Ser Cys Lys Asn Val Pro Ala Gly Ala Ser Cys * 355 360 63 364 PRT Aspergillus 63 Met His Phe Phe Gln Ser Ser Leu Val Ala Ala Thr Met Gly Ala Ala 1 5 10 15 Leu Val Ala Ala Ala Pro Ala Ala Asp Leu Glu Thr Arg Gly Ser Cys 20 25 30 Thr Phe Thr Ser Thr Ser Ala Leu Lys Ser Gly Lys Ala Ser Cys Ser 35 40 45 Thr Ile Thr Leu Gln Asn Ile Ala Val Pro Ala Gly Glu Thr Leu Asp 50 55 60 Leu Thr Gly Leu Lys Ala Gly Thr Thr Val Val Phe Asp Gly Thr Thr 65 70 75 80 Thr Phe Gly Tyr Lys Glu Trp Glu Gly Pro Leu Ile Ser Ala Ser Gly 85 90 95 Thr Ser Ile Thr Ile Lys Gln Asn Pro Gly Ala Lys Ile Asp Cys Asp 100 105 110 Gly Ala Arg Trp Trp Asp Gly Lys Gly Gly Asn Gly Gly Lys Lys Lys 115 120 125 Pro Lys Phe Phe Ser Ala His Lys Leu Asn Lys Ser Asn Ile Thr Gly 130 135 140 Leu Lys Val Tyr Asn Thr Pro Val His Gly Phe Ser Ile Gln Ser Asp 145 150 155 160 His Leu Thr Ile Lys Asp Val Leu Leu Asp Asn Ser Ala Gly Thr Lys 165 170 175 Leu Gly His Asn Thr Asp Ala Phe Asp Val Gly Ser Ser Thr Tyr Ile 180 185 190 Thr Ile Asp Gly Ala Thr Val Tyr Asn Gln Asp Asp Cys Leu Ala Val 195 200 205 Asn Ser Gly Glu His Ile Thr Phe Thr Asn Gly Tyr Cys Asn Gly Gly 210 215 220 His Gly Leu Ser Ile Gly Ser Val Gly Gly Arg Ser Asn Asn Val Val 225 230 235 240 Asn Asp Val Thr Ile Ser Asn Ser Gln Val Ile Asn Ser Gln Asn Gly 245 250 255 Ala Arg Ile Lys Thr Val Tyr Gly Ala Thr Gly Ser Val Thr Gly Val 260 265 270 Lys Phe Gln Asp Ile Ser Leu Lys Gly Ile Thr Lys Tyr Gly Ile Val 275 280 285 Val Gln Gln Asp Tyr Glu Asn Gly Lys Pro Thr Gly Lys Pro Thr Asn 290 295 300 Gly Val Lys Val Ser Asp Ile Thr Phe Glu Lys Val Thr Gly Thr Val 305 310 315 320 Thr Ser Ser Ala Thr Asp Ile Tyr Ile Leu Cys Gly Ser Gly Ser Cys 325 330 335 Thr Asn Trp Thr Trp Ser Gly Asn Ser Val Thr Gly Gly Lys Lys Ser 340 345 350 Ser Ser Cys Lys Asn Val Pro Ala Gly Ala Ser Cys 355 360 64 712 DNA Aspergillus 64 atggtctcat tctcttctct cgttctcgct gcctccaccg ttgctggcgt gctagctaca 60 cccggctcgg agcaatacgt tgagctagcc aagcggcagc tcaccagctc tcagactggc 120 acgaataacg gctactacta ctccttctgg accgacggcg gcggccaggt gacctacacc 180 aacggcaatg gcggccagta tcaggtcgac tggaacaact gcggcaactt tgttgctggg 240 aagggctgga acccggccag cgagaagtat gcgtcctctc cctgcttgtt aggttcaagc 300 taatggattc agagcggtca cctacagcgg ctcctggcag accagcggaa acggctacct 360 ctccgtgtac ggctggacga ccagtccgct ggtcgaattc tacatcgtgg agagttacgg 420 ctcctatgac ccctccacgg gagccaccca tctcggcacc gtcgagagcg acggggccac 480 gtacaacctc tacaagacga cgcggacgaa tgcgccgtcc atccagggca cggctacttt 540 tgaccagtac tggtcggttc ggacttcgca ccggcagagt ggaactgtga cgacgaagaa 600 ccactttgat gcgtggagaa atgcgggtct gcaattgggg aactttgact atatgattgt 660 tgcgacggag gggtaccaga gcagcggctc tgctactatc actgtttctt ag 712 65 666 DNA Aspergillus CDS (1)...(666) 65 atg gtc tca ttc tct tct ctc gtt ctc gct gcc tcc acc gtt gct ggc 48 Met Val Ser Phe Ser Ser Leu Val Leu Ala Ala Ser Thr Val Ala Gly 1 5 10 15 gtg cta gct aca ccc ggc tcg gag caa tac gtt gag cta gcc aag cgg 96 Val Leu Ala Thr Pro Gly Ser Glu Gln Tyr Val Glu Leu Ala Lys Arg 20 25 30 cag ctc acc agc tct cag act ggc acg aat aac ggc tac tac tac tcc 144 Gln Leu Thr Ser Ser Gln Thr Gly Thr Asn Asn Gly Tyr Tyr Tyr Ser 35 40 45 ttc tgg acc gac ggc ggc ggc cag gtg acc tac acc aac ggc aat ggc 192 Phe Trp Thr Asp Gly Gly Gly Gln Val Thr Tyr Thr Asn Gly Asn Gly 50 55 60 ggc cag tat cag gtc gac tgg aac aac tgc ggc aac ttt gtt gct ggg 240 Gly Gln Tyr Gln Val Asp Trp Asn Asn Cys Gly Asn Phe Val Ala Gly 65 70 75 80 aag ggc tgg aac ccg gcc agc gag aaa gcg gtc acc tac agc ggc tcc 288 Lys Gly Trp Asn Pro Ala Ser Glu Lys Ala Val Thr Tyr Ser Gly Ser 85 90 95 tgg cag acc agc gga aac ggc tac ctc tcc gtg tac ggc tgg acg acc 336 Trp Gln Thr Ser Gly Asn Gly Tyr Leu Ser Val Tyr Gly Trp Thr Thr 100 105 110 agt ccg ctg gtc gaa ttc tac atc gtg gag agt tac ggc tcc tat gac 384 Ser Pro Leu Val Glu Phe Tyr Ile Val Glu Ser Tyr Gly Ser Tyr Asp 115 120 125 ccc tcc acg gga gcc acc cat ctc ggc acc gtc gag agc gac ggg gcc 432 Pro Ser Thr Gly Ala Thr His Leu Gly Thr Val Glu Ser Asp Gly Ala 130 135 140 acg tac aac ctc tac aag acg acg cgg acg aat gcg ccg tcc atc cag 480 Thr Tyr Asn Leu Tyr Lys Thr Thr Arg Thr Asn Ala Pro Ser Ile Gln 145 150 155 160 ggc acg gct act ttt gac cag tac tgg tcg gtt cgg act tcg cac cgg 528 Gly Thr Ala Thr Phe Asp Gln Tyr Trp Ser Val Arg Thr Ser His Arg 165 170 175 cag agt gga act gtg acg acg aag aac cac ttt gat gcg tgg aga aat 576 Gln Ser Gly Thr Val Thr Thr Lys Asn His Phe Asp Ala Trp Arg Asn 180 185 190 gcg ggt ctg caa ttg ggg aac ttt gac tat atg att gtt gcg acg gag 624 Ala Gly Leu Gln Leu Gly Asn Phe Asp Tyr Met Ile Val Ala Thr Glu 195 200 205 ggg tac cag agc agc ggc tct gct act atc act gtt tct tag 666 Gly Tyr Gln Ser Ser Gly Ser Ala Thr Ile Thr Val Ser * 210 215 220 66 221 PRT Aspergillus 66 Met Val Ser Phe Ser Ser Leu Val Leu Ala Ala Ser Thr Val Ala Gly 1 5 10 15 Val Leu Ala Thr Pro Gly Ser Glu Gln Tyr Val Glu Leu Ala Lys Arg 20 25 30 Gln Leu Thr Ser Ser Gln Thr Gly Thr Asn Asn Gly Tyr Tyr Tyr Ser 35 40 45 Phe Trp Thr Asp Gly Gly Gly Gln Val Thr Tyr Thr Asn Gly Asn Gly 50 55 60 Gly Gln Tyr Gln Val Asp Trp Asn Asn Cys Gly Asn Phe Val Ala Gly 65 70 75 80 Lys Gly Trp Asn Pro Ala Ser Glu Lys Ala Val Thr Tyr Ser Gly Ser 85 90 95 Trp Gln Thr Ser Gly Asn Gly Tyr Leu Ser Val Tyr Gly Trp Thr Thr 100 105 110 Ser Pro Leu Val Glu Phe Tyr Ile Val Glu Ser Tyr Gly Ser Tyr Asp 115 120 125 Pro Ser Thr Gly Ala Thr His Leu Gly Thr Val Glu Ser Asp Gly Ala 130 135 140 Thr Tyr Asn Leu Tyr Lys Thr Thr Arg Thr Asn Ala Pro Ser Ile Gln 145 150 155 160 Gly Thr Ala Thr Phe Asp Gln Tyr Trp Ser Val Arg Thr Ser His Arg 165 170 175 Gln Ser Gly Thr Val Thr Thr Lys Asn His Phe Asp Ala Trp Arg Asn 180 185 190 Ala Gly Leu Gln Leu Gly Asn Phe Asp Tyr Met Ile Val Ala Thr Glu 195 200 205 Gly Tyr Gln Ser Ser Gly Ser Ala Thr Ile Thr Val Ser 210 215 220 67 739 DNA Aspergillus 67 atggtttctt tctcctacct gctgctggcg tgctccgcca ttggagctct ggctgccccc 60 gtcgaacccg agaccacctc gttcaatgag actgctcttc atgagttcgc tgagcgcgcc 120 ggcaccccaa gctccaccgg ctggaacaac ggctactact actccttctg gactgatggc 180 ggcggcgacg tgacctacac caatggcgcc ggtggctcgt actccgtcaa ctggaggaac 240 gtgggcaact ttgtcggtgg aaagggctgg aaccctggaa gcgctaggta ccgagctttg 300 tcaacgtcgg atgtgcagac ctgtggctga cagaagtaga accatcaact acggaggcag 360 cttcaacccc agcggcaatg gctacctggc tgtctacggc tggaccacca accccttgat 420 tgagtactac gttgttgagt cgtatggtac atacaacccc ggcagcggcg gtaccttcag 480 gggcactgtc aacaccgacg gtggcactta caacatctac acggccgttc gctacaatgc 540 tccctccatc gaaggcacca agaccttcac ccagtactgg tctgtgcgca cctccaagcg 600 taccggcggc actgtcacca tggccaacca cttcaacgcc tggagcagac tgggcatgaa 660 cctgggaact cacaactacc agattgtcgc cactgagggt taccagagca gcggatctgc 720 ttccatcact gtctactag 739 68 705 DNA Aspergillus CDS (1)...(705) 68 atg gtt tct ttc tcc tac ctg ctg ctg gcg tgc tcc gcc att gga gct 48 Met Val Ser Phe Ser Tyr Leu Leu Leu Ala Cys Ser Ala Ile Gly Ala 1 5 10 15 ctg gct gcc ccc gtc gaa ccc gag acc acc tcg ttc aat gag act gct 96 Leu Ala Ala Pro Val Glu Pro Glu Thr Thr Ser Phe Asn Glu Thr Ala 20 25 30 ctt cat gag ttc gct gag cgc gcc ggc acc cca agc tcc acc ggc tgg 144 Leu His Glu Phe Ala Glu Arg Ala Gly Thr Pro Ser Ser Thr Gly Trp 35 40 45 aac aac ggc tac tac tac tcc ttc tgg act gat ggc ggc ggc gac gtg 192 Asn Asn Gly Tyr Tyr Tyr Ser Phe Trp Thr Asp Gly Gly Gly Asp Val 50 55 60 acc tac acc aat ggc gcc ggt ggc tcg tac tcc gtc aac tgg agg aac 240 Thr Tyr Thr Asn Gly Ala Gly Gly Ser Tyr Ser Val Asn Trp Arg Asn 65 70 75 80 gtg ggc aac ttt gtc ggt gga aag ggc tgg aac cct gga agc gct agg 288 Val Gly Asn Phe Val Gly Gly Lys Gly Trp Asn Pro Gly Ser Ala Arg 85 90 95 tac cga gct tta agt aga acc atc aac tac gga ggc agc ttc aac ccc 336 Tyr Arg Ala Leu Ser Arg Thr Ile Asn Tyr Gly Gly Ser Phe Asn Pro 100 105 110 agc ggc aat ggc tac ctg gct gtc tac ggc tgg acc acc aac ccc ttg 384 Ser Gly Asn Gly Tyr Leu Ala Val Tyr Gly Trp Thr Thr Asn Pro Leu 115 120 125 att gag tac tac gtt gtt gag tcg tat ggt aca tac aac ccc ggc agc 432 Ile Glu Tyr Tyr Val Val Glu Ser Tyr Gly Thr Tyr Asn Pro Gly Ser 130 135 140 ggc ggt acc ttc agg ggc act gtc aac acc gac ggt ggc act tac aac 480 Gly Gly Thr Phe Arg Gly Thr Val Asn Thr Asp Gly Gly Thr Tyr Asn 145 150 155 160 atc tac acg gcc gtt cgc tac aat gct ccc tcc atc gaa ggc acc aag 528 Ile Tyr Thr Ala Val Arg Tyr Asn Ala Pro Ser Ile Glu Gly Thr Lys 165 170 175 acc ttc acc cag tac tgg tct gtg cgc acc tcc aag cgt acc ggc ggc 576 Thr Phe Thr Gln Tyr Trp Ser Val Arg Thr Ser Lys Arg Thr Gly Gly 180 185 190 act gtc acc atg gcc aac cac ttc aac gcc tgg agc aga ctg ggc atg 624 Thr Val Thr Met Ala Asn His Phe Asn Ala Trp Ser Arg Leu Gly Met 195 200 205 aac ctg gga act cac aac tac cag att gtc gcc act gag ggt tac cag 672 Asn Leu Gly Thr His Asn Tyr Gln Ile Val Ala Thr Glu Gly Tyr Gln 210 215 220 agc agc gga tct gct tcc atc act gtc tac tag 705 Ser Ser Gly Ser Ala Ser Ile Thr Val Tyr * 225 230 69 234 PRT Aspergillus 69 Met Val Ser Phe Ser Tyr Leu Leu Leu Ala Cys Ser Ala Ile Gly Ala 1 5 10 15 Leu Ala Ala Pro Val Glu Pro Glu Thr Thr Ser Phe Asn Glu Thr Ala 20 25 30 Leu His Glu Phe Ala Glu Arg Ala Gly Thr Pro Ser Ser Thr Gly Trp 35 40 45 Asn Asn Gly Tyr Tyr Tyr Ser Phe Trp Thr Asp Gly Gly Gly Asp Val 50 55 60 Thr Tyr Thr Asn Gly Ala Gly Gly Ser Tyr Ser Val Asn Trp Arg Asn 65 70 75 80 Val Gly Asn Phe Val Gly Gly Lys Gly Trp Asn Pro Gly Ser Ala Arg 85 90 95 Tyr Arg Ala Leu Ser Arg Thr Ile Asn Tyr Gly Gly Ser Phe Asn Pro 100 105 110 Ser Gly Asn Gly Tyr Leu Ala Val Tyr Gly Trp Thr Thr Asn Pro Leu 115 120 125 Ile Glu Tyr Tyr Val Val Glu Ser Tyr Gly Thr Tyr Asn Pro Gly Ser 130 135 140 Gly Gly Thr Phe Arg Gly Thr Val Asn Thr Asp Gly Gly Thr Tyr Asn 145 150 155 160 Ile Tyr Thr Ala Val Arg Tyr Asn Ala Pro Ser Ile Glu Gly Thr Lys 165 170 175 Thr Phe Thr Gln Tyr Trp Ser Val Arg Thr Ser Lys Arg Thr Gly Gly 180 185 190 Thr Val Thr Met Ala Asn His Phe Asn Ala Trp Ser Arg Leu Gly Met 195 200 205 Asn Leu Gly Thr His Asn Tyr Gln Ile Val Ala Thr Glu Gly Tyr Gln 210 215 220 Ser Ser Gly Ser Ala Ser Ile Thr Val Tyr 225 230 70 1002 DNA Aspergillus 70 atgatctcca tttcctcgct cagctttgga ctcgccgcta tcgccggcgc atatgctctt 60 ccgagtgaca aatccgtcag cttagcggaa cgtcagacga tcacgaccag ccagacaggc 120 acaaacaatg gctactacta ttccttctgg accaacggtg ccggatcagt gcaatataca 180 aatggtgctg gtggcgaata tagtgtgacg tgggcgaacc agaacggtgg tgactttacc 240 tgtgggaagg gctggaatcc agggagtgac cagtaggcaa cgccccagaa ctatagaaga 300 ggacgcaaag aaagcactaa actctctact agtgacatta ccttctctgg cagcttcaat 360 ccttccggaa atgcttacct gtccgtgtat ggatggacta ccaaccccct agtcgaatac 420 tacatcctcg agaactatgg cagttacaat cctggctcgg gcatgacgca caagggcacc 480 gtcaccagcg atggatccac ctacgacatc tatgagcacc aacaggtcaa ccagccttcg 540 atcgtcggca cggccacctt caaccaatac tggtccatcc gccaaaacaa gcgatccagc 600 ggcacagtca ccaccgcgaa tcacttcaag gcctgggcta gtctggggat gaacctgggt 660 acccataact atcagattgt ttccactgag ggatatgaga gcagcggtac ctcgaccatc 720 actgtctcgt ctggtggttc ttcttctggt ggaagtggtg gcagctcgtc tactacttcc 780 tcaggcagct cccctactgg tggctccggc agtgtaagtc ttcttccata tggttgtggc 840 tttatgtgta ttctgactgt gatagtgctc tgctttgtgg ggccagtgcg gtggaattgg 900 ctggtctggt cctacttgct gctcttcggg cacttgccag gtttcgaact cgtactactc 960 ccagtgcttg tagtaccttc ttgcagggtt atatccaagt ga 1002 71 942 DNA Aspergillus CDS (1)...(942) 71 atg atc tcc att tcc tcg ctc agc ttt gga ctc gcc gct atc gcc ggc 48 Met Ile Ser Ile Ser Ser Leu Ser Phe Gly Leu Ala Ala Ile Ala Gly 1 5 10 15 gca tat gct ctt ccg agt gac aaa tcc gtc agc tta gcg gaa cgt cag 96 Ala Tyr Ala Leu Pro Ser Asp Lys Ser Val Ser Leu Ala Glu Arg Gln 20 25 30 acg atc acg acc agc cag aca ggc aca aac aat ggc tac tac tat tcc 144 Thr Ile Thr Thr Ser Gln Thr Gly Thr Asn Asn Gly Tyr Tyr Tyr Ser 35 40 45 ttc tgg acc aac ggt gcc gga tca gtg caa tat aca aat ggt gct ggt 192 Phe Trp Thr Asn Gly Ala Gly Ser Val Gln Tyr Thr Asn Gly Ala Gly 50 55 60 ggc gaa tat agt gtg acg tgg gcg aac cag aac ggt ggt gac ttt acc 240 Gly Glu Tyr Ser Val Thr Trp Ala Asn Gln Asn Gly Gly Asp Phe Thr 65 70 75 80 tgt ggg aag ggc tgg aat cca ggg agt gac cat gac att acc ttc tct 288 Cys Gly Lys Gly Trp Asn Pro Gly Ser Asp His Asp Ile Thr Phe Ser 85 90 95 ggc agc ttc aat cct tcc gga aat gct tac ctg tcc gtg tat gga tgg 336 Gly Ser Phe Asn Pro Ser Gly Asn Ala Tyr Leu Ser Val Tyr Gly Trp 100 105 110 act acc aac ccc cta gtc gaa tac tac atc ctc gag aac tat ggc agt 384 Thr Thr Asn Pro Leu Val Glu Tyr Tyr Ile Leu Glu Asn Tyr Gly Ser 115 120 125 tac aat cct ggc tcg ggc atg acg cac aag ggc acc gtc acc agc gat 432 Tyr Asn Pro Gly Ser Gly Met Thr His Lys Gly Thr Val Thr Ser Asp 130 135 140 gga tcc acc tac gac atc tat gag cac caa cag gtc aac cag cct tcg 480 Gly Ser Thr Tyr Asp Ile Tyr Glu His Gln Gln Val Asn Gln Pro Ser 145 150 155 160 atc gtc ggc acg gcc acc ttc aac caa tac tgg tcc atc cgc caa aac 528 Ile Val Gly Thr Ala Thr Phe Asn Gln Tyr Trp Ser Ile Arg Gln Asn 165 170 175 aag cga tcc agc ggc aca gtc acc acc gcg aat cac ttc aag gcc tgg 576 Lys Arg Ser Ser Gly Thr Val Thr Thr Ala Asn His Phe Lys Ala Trp 180 185 190 gct agt ctg ggg atg aac ctg ggt acc cat aac tat cag att gtt tcc 624 Ala Ser Leu Gly Met Asn Leu Gly Thr His Asn Tyr Gln Ile Val Ser 195 200 205 act gag gga tat gag agc agc ggt acc tcg acc atc act gtc tcg tct 672 Thr Glu Gly Tyr Glu Ser Ser Gly Thr Ser Thr Ile Thr Val Ser Ser 210 215 220 ggt ggt tct tct tct ggt gga agt ggt ggc agc tcg tct act act tcc 720 Gly Gly Ser Ser Ser Gly Gly Ser Gly Gly Ser Ser Ser Thr Thr Ser 225 230 235 240 tca ggc agc tcc cct act ggt ggc tcc ggc agt gta agt ctt ctt cca 768 Ser Gly Ser Ser Pro Thr Gly Gly Ser Gly Ser Val Ser Leu Leu Pro 245 250 255 tat ggt tgt ggc ttt atg tgt att ctg act gtg ata gtg ctc tgc ttt 816 Tyr Gly Cys Gly Phe Met Cys Ile Leu Thr Val Ile Val Leu Cys Phe 260 265 270 gtg ggg cca gtg cgg tgg aat tgg ctg gtc tgg tcc tac ttg ctg ctc 864 Val Gly Pro Val Arg Trp Asn Trp Leu Val Trp Ser Tyr Leu Leu Leu 275 280 285 ttc ggg cac ttg cca ggt ttc gaa ctc gta cta ctc cca gtg ctt gta 912 Phe Gly His Leu Pro Gly Phe Glu Leu Val Leu Leu Pro Val Leu Val 290 295 300 gta cct tct tgc agg gtt ata tcc aag tga 942 Val Pro Ser Cys Arg Val Ile Ser Lys * 305 310 72 313 PRT Aspergillus 72 Met Ile Ser Ile Ser Ser Leu Ser Phe Gly Leu Ala Ala Ile Ala Gly 1 5 10 15 Ala Tyr Ala Leu Pro Ser Asp Lys Ser Val Ser Leu Ala Glu Arg Gln 20 25 30 Thr Ile Thr Thr Ser Gln Thr Gly Thr Asn Asn Gly Tyr Tyr Tyr Ser 35 40 45 Phe Trp Thr Asn Gly Ala Gly Ser Val Gln Tyr Thr Asn Gly Ala Gly 50 55 60 Gly Glu Tyr Ser Val Thr Trp Ala Asn Gln Asn Gly Gly Asp Phe Thr 65 70 75 80 Cys Gly Lys Gly Trp Asn Pro Gly Ser Asp His Asp Ile Thr Phe Ser 85 90 95 Gly Ser Phe Asn Pro Ser Gly Asn Ala Tyr Leu Ser Val Tyr Gly Trp 100 105 110 Thr Thr Asn Pro Leu Val Glu Tyr Tyr Ile Leu Glu Asn Tyr Gly Ser 115 120 125 Tyr Asn Pro Gly Ser Gly Met Thr His Lys Gly Thr Val Thr Ser Asp 130 135 140 Gly Ser Thr Tyr Asp Ile Tyr Glu His Gln Gln Val Asn Gln Pro Ser 145 150 155 160 Ile Val Gly Thr Ala Thr Phe Asn Gln Tyr Trp Ser Ile Arg Gln Asn 165 170 175 Lys Arg Ser Ser Gly Thr Val Thr Thr Ala Asn His Phe Lys Ala Trp 180 185 190 Ala Ser Leu Gly Met Asn Leu Gly Thr His Asn Tyr Gln Ile Val Ser 195 200 205 Thr Glu Gly Tyr Glu Ser Ser Gly Thr Ser Thr Ile Thr Val Ser Ser 210 215 220 Gly Gly Ser Ser Ser Gly Gly Ser Gly Gly Ser Ser Ser Thr Thr Ser 225 230 235 240 Ser Gly Ser Ser Pro Thr Gly Gly Ser Gly Ser Val Ser Leu Leu Pro 245 250 255 Tyr Gly Cys Gly Phe Met Cys Ile Leu Thr Val Ile Val Leu Cys Phe 260 265 270 Val Gly Pro Val Arg Trp Asn Trp Leu Val Trp Ser Tyr Leu Leu Leu 275 280 285 Phe Gly His Leu Pro Gly Phe Glu Leu Val Leu Leu Pro Val Leu Val 290 295 300 Val Pro Ser Cys Arg Val Ile Ser Lys 305 310 

What is claimed is:
 1. An isolated nucleic acid molecule comprising (a) a nucleotide sequence that encodes a polypeptide, said polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72; or (b) a complement of (a).
 2. An isolated nucleic acid molecule comprising (a) a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70; or (b) a complement of (a).
 3. An isolated nucleic acid molecule comprising a nucleotide sequence that hybridizes under medium stringency conditions to a nucleic acid probe consisting of: (a) a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, 70, 73, 76, and 79; (b) a nucleotide sequence that encodes a polypeptide consisting of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72; or (c) the complement of the nucleotide sequence of (a), or (b); wherein said medium stringency conditions comprise hybridization to filter-bound DNA in 6×sodium chloride/sodium citrate (SSC) at about 45° C. followed by one or more washes in 0.2×SSC/0.1% SDS at about 50 to about 65° C.
 4. The isolated nucleic acid molecule of claim 1, 2, or 3, which is genomic DNA.
 5. The isolated nucleic acid molecule of claim 1, 2, or 3, which is cDNA.
 6. The isolated nucleic acid molecule of claim 1, 2, or 3, which is RNA.
 7. The isolated nucleic acid molecule of claim 1, 2, or 3, which is single-stranded.
 8. An isolated nucleic acid molecule comprising at least 8 consecutive nucleotides of: (a) a nucleotide sequence that encodes a polypeptide, said polypeptide consisting of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72; (b) a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70; or (c) the complement of the nucleotide sequence of (a), or (b).
 9. A nucleic acid probe consisting of at least 8 nucleotides, wherein the nucleic acid probe is hybridizable under medium stringency conditions to at least a portion of: (a) a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and 70; or (b) the complement of the nucleotide sequence of (a) wherein said medium stringency conditions comprise hybridization to filter-bound DNA in 6×sodium chloride/sodium citrate (SSC) at about 45° C. followed by one or more washes in 0.2×SSC/0.1% SDS at about 50 to 65° C.
 10. A nucleic acid molecule comprising a nucleotide sequence of claim 1, 2, or 3 uninterrupted by stop codons within a coding sequence that encodes a heterologous protein or peptide.
 11. A recombinant vector comprising the nucleic acid molecule of claim 1, 2, 3, 8, or
 10. 12. An expression construct comprising the nucleic acid molecule of claim 1, 2, 3, 8, or 10, wherein the nucleotide sequence is operatively associated with a regulatory nucleotide sequence containing transcriptional and/or translational regulatory signals that controls expression of the nucleotide sequence in a host cell.
 13. A genetically engineered host cell comprising the nucleic acid molecule of claim 1, 2, 3, 6, 7, 8, or
 10. 14. A genetically engineered host cell comprising the nucleic acid molecule of claim 1, 2, 3, 8, or 10, wherein the nucleotide sequence is operatively associated with a regulatory nucleotide sequence containing transcriptional and/or translational regulatory information that controls expression of the nucleotide sequence in the host cell.
 15. A method for detecting in a sample the presence of a nucleic acid molecule that encodes an enzyme, said method comprising: (a) contacting the sample with a nucleic acid probe of claim 9 under hybridizing conditions; and (b) measuring the hybridization of the probe to the nucleic acids of the sample, thereby detecting the presence of the nucleic acid molecule.
 16. A method of making a polypeptide comprising the steps of: (a) culturing the cell of claim 14 under the appropriate conditions to produce the polypeptide; and (b) isolating the polypeptide.
 17. An isolated polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, 72, 75, 78, and
 81. 18. An isolated polypeptide comprising an amino acid sequence encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 2, 5, 8, 11, 14, 17, 20, 23, 26, 29, 32, 35, 38, 41, 44, 47, 50, 53, 56, 59, 62, 65, 68, 71, 1, 4, 7, 10, 13, 16, 19, 22, 25, 28, 31, 34, 37, 40, 43, 46, 49, 52, 55, 58, 61, 64, 67, and
 70. 19. An isolated polypeptide, the amino acid sequence of which comprises at least six consecutive residues of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and
 72. 20. An isolated polypeptide, the amino acid sequence of which is selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72 with at least one conservative amino acid substitution.
 21. An isolated polypeptide comprising an amino acid sequence which is at least 60% identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, and displays the catalytic activity of an enzyme selected from the group consisting of tannase, cellulase, glucose oxidase, glucoamylase, phytase, β-galactosidases, invertase, lipase, α-amylase, laccase, polygalacturonase and xylanase.
 22. A chimeric protein comprising a polypeptide of claim 19 fused via a covalent bond to an amino acid sequence of a second polypeptide.
 23. An enzymatic composition comprising the polypeptide of claim 17, 18, or
 21. 24. The enzymatic composition of claim 23, wherein the composition is in solid form.
 25. The enzymatic composition of claim 23 further comprising one or more solid phase, wherein the polypeptide is present on the solid phase.
 26. An enzymatic composition comprising (a) a lysate of the genetically engineered cells of claim 14, or (b) a culture medium in which the genetically engineered cells of claim 14 were cultured.
 27. An enzymatic composition enriched for a polypeptide which is at least 60% identical to the polypeptide, the amino acid sequence of which is selected from the group consisting of SEQ ID NO: 3, 6, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36, 39, 42, 45, 48, 51, 54, 57, 60, 63, 66, 69, and 72, and displays the catalytic activity of an enzyme selected from the group consisting of tannase, cellulase, glucose oxidase, glucoamylase, phytase, β-galactosidases, invertase, lipase, α-amylase, laccase, polygalacturonase and xylanase.
 28. An antibody preparation which binds to the polypeptide of claim
 17. 29. A molecule comprising a fragment of the antibody of claim 28, which fragment binds to the polypeptide of claim 17
 30. The antibody preparation of claim 28 which comprises a monoclonal antibody.
 31. A kit comprising in one or more containers the enzymatic composition of claim
 23. 32. A method for modulating the amount of compounds that comprise a gallate ester linkage in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 3 and 6, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 1, 2, 4, and 5; or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a tannase.
 33. A method for modulating the amount of cellulose in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising the amino acid sequence of SEQ ID NO: 9, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 7 and 8, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a cellulase.
 34. A method for modulating the amount of glucose or oxygen in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 12, 15, and 18, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 10, 11, 13, 14, 16, and 17, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a glucose oxidase.
 35. A method for modulating the amount of myo-inositol phosphates in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising the amino acid sequence of SEQ ID NO: 24, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 22 and 23, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a phytase.
 36. A method for modulating the amount of lactose in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 27 and 30, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 25, 26, 28, and 29, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a β-galactosidase.
 37. A method for modulating the amount of sucrose in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising the amino acid sequence of SEQ ID NO: 36, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 34 and 35, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of an invertase.
 38. A method for modulating the amount of glyceride in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising the amino acid sequence of SEQ ID NO: 39, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 37 and 38, or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a lipase.
 39. A method for modulating the amount of starches or maltodextrins in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 42, 45, and 48, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 40, 41, 43, 44, 46 and 47; or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of an α-amylase.
 40. A method for modulating the amount of oxidated phenolic compounds in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising the amino acid sequence of SEQ ID NO: 51, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 49 and 50; or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a laccase.
 41. A method for modulating the amount of high molecular weight polygalacturonic acid chains or low molecular weight polygalacturonic acid chains in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 57, 60 and 63, (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 55, 56, 58, 59, 61 and 62; or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a polygalacturonase.
 42. A method for modulating the amount of xylan or xylo-oligomers in a composition comprising contacting the composition with an enzymatic composition, wherein the enzymatic composition comprises (a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 66, 69, and 72; (b) a polypeptide encoded by a nucleotide sequence selected from the group consisting of SEQ ID NO: 64, 65, 67, 68, 70, and 71; or (c) a polypeptide comprising an amino acid sequence which is at least 60% identical to the amino acid sequence of the polypeptide of (a) and displays the catalytic activity of a xylanase.
 43. A method for identifying a compound that modulates the activity of an enzyme, comprising: (a) contacting a test compound with an enzymatic composition of claim 23; and (b) detecting a change in the activity of the enzyme as compared to an enzymatic composition that is not contacted with the test compound; wherein the activity of the enzyme is that of an enzyme selected from the group consisting of tannase, cellulase, glucose oxidase, glucoamylase, phytase, β-galactosidases, invertase, lipase, α-amylase, laccase, polygalacturonase and xylanase.
 44. A method for identifying an enzyme with modified chemical and/or physical characteristics, comprising: (a) mutagenizing a nucleotide sequence that encodes the enzyme; and (b) determining the chemical and/or physical characteristics of the enzyme produced as a result of expression of the mutagenized nucleotide sequence.
 45. The method of claim 44 wherein the mutagenizing step comprises using portions of the nucleotide sequence of another enzyme that is imperfectly matched to the nucleotide sequence of the enzyme in a sequence alignment. 